Score |
Strand | Gene name |
Blattner ID |
Description |
EcoCyc link |
SwissProt comment |
| 1.654300 | + | dfp | b3639 | flavoprotein affecting synthesis of DNA and pantothenate metabolism |
EG10004 |
FUNCTION: FLAVOPROTEIN AFFECTING SYNTHESIS OF DNA AND PANTOTHENATE
METABOLISM.
|
 | | dut | b3640 | deoxyuridinetriphosphatase |
EG10251 |
FUNCTION: THIS ENZYME IS INVOLVED IN NUCLEOTIDE METABOLISM: IT
PRODUCES DUMP, THE IMMEDIATE PRECURSOR OF THYMIDINE NUCLEOTIDES
AND IT DECREASES THE INTRACELLULAR CONCENTRATION OF DUTP SO THAT
URACIL CANNOT BE INCORPORATED INTO DNA.
CATALYTIC ACTIVITY: DUTP + H(2)O = DUMP + PYROPHOSPHATE.
PATHWAY: DE NOVO SYNTHESIS OF THYMIDYLATE.
SUBUNIT: HOMOTRIMER.
SIMILARITY: BELONGS TO THE DUTPASE FAMILY.
|
| | ttk | b3641 | putative transcriptional regulator |
EG11191 |
FUNCTION: UNKNOWN.
SIMILARITY: BELONGS TO THE TETR/ACRR FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 1.364239 | + | b0878 | b0878 | putative membrane protein |
EG13694 |
SIMILARITY: BELONGS TO THE ACRA/ACRE FAMILY.
|
| | ybjZ | b0879 | putative ATP-binding component of a transport system |
EG13695 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: BELONGS TO THE ATP-BINDING TRANSPORT PROTEIN FAMILY
(ABC TRANSPORTERS).
|
| 1.345683 | + | yicP | b3665 | probable adenine deaminase (synthesis xanthine) |
EG11692 |
CATALYTIC ACTIVITY: ADENINE + H(2)O = HYPOXANTHINE + NH(3).
SIMILARITY: BELONGS TO THE ADENINE AMINASE FAMILY.
|
| 1.254524 | - | smf_2 | b3285 | orf, fragment 2 |
EG11604 |
SIMILARITY: BELONGS TO THE SMF FAMILY.
CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO A
FRAMESHIFT IN POSITION 249.
|
| | smg | b3284 | orf, hypothetical protein |
EG11605 |
|
| | yrdD | b3283 | putative DNA topoisomerase |
EG12841 |
SIMILARITY: STRONG, TO H.INFLUENZAE HI0656.1.
SIMILARITY: STRONG, TO THE C-TERMINUS OF SOME BACTERIAL
TOPOISOMERASE I.
SIMILARITY: SOME, TO M.JANNASCHII MJ0664.
|
| | yrdC | b3282 | orf, hypothetical protein |
EG12840 |
SIMILARITY: BELONGS TO THE SUA5/YRDC/YCIO/YWLC FAMILY. STRONG, TO
H.INFLUENZAE HI0656.
|
| | aroE | b3281 | dehydroshikimate reductase |
EG10077 |
CATALYTIC ACTIVITY: SHIKIMATE + NADP(+) = 5-DEHYDROSHIKIMATE +
NADPH.
PATHWAY: FOURTH STEP IN THE BIOSYNTHESIS OF CHORISMATE WITHIN THE
BIOSYNTHESIS OF AROMATIC AMINO ACIDS (THE SHIKIMATE PATHWAY).
SUBUNIT: MONOMER.
SIMILARITY: BELONGS TO THE SHIKIMATE DEHYDROGENASE FAMILY.
|
| | yrdB | b3280 | orf, hypothetical protein |
EG12839 |
|
| 0.894973 | + | nadB | b2574 | quinolinate synthetase, B protein |
EG10631 |
FUNCTION: CATALYZES THE OXIDATION OF L-ASPARTATE TO IMINOASPARTATE
WHICH IS CONDENSED WITH DIHYDROXYACETONE PHOSPHATE TO QUINOLINATE
UNDER THE ACTION OF QUINOLINATE SYNTHASE A.
CATALYTIC ACTIVITY: L-ASPARTATE + H(2)O + O(2) = OXALOACETATE +
NH(3) + H(2)O(2).
COFACTOR: FAD.
PATHWAY: QUINOLINATE (PYRIDINE-2,3-DICARBOXYLATE) BIOSYNTHESIS
(NOTE: QUINOLINATE FORMATION OCCURS VIA 4 DIFFERENT PATHWAYS
DEPENDING ON THE ORGANISM). INVOLVED IN DE NOVO BIOSYNTHESIS OF
NAD.
SUBUNIT: HETERODIMER. THE QUINOLINATE SYNTHETASE COMPLEX CONSISTS
OF THE TWO ENZYMES QUINOLINATE SYNTHETASE A AND B.
PTM: TWO DISULFIDE BONDS ARE PRESENT.
|
| 0.826779 | - | b1657 | b1657 | putative transport protein |
|
|
| 0.783068 | + | b1458 | b1458 | orf, hypothetical protein |
|
|
| | b1459 | b1459 | orf, hypothetical protein |
|
|
| 0.771039 | + | hisL | b2018 | his operon leader peptide |
EG11269 |
FUNCTION: THIS PROTEIN IS INVOLVED IN THE ATTENUATION MECHANISM
FOR THE CONTROL OF THE EXPRESSION OF THE HIS STRUCTURAL GENES.
|
| | hisG | b2019 | ATP phosphoribosyltransferase |
EG10449 |
CATALYTIC ACTIVITY: 1-(5-PHOSPHO-D-RIBOSYL)-ATP + PYROPHOSPHATE =
ATP + 5-PHOSPHO-ALPHA-D-RIBOSE 1-DIPHOSPHATE.
PATHWAY: FIRST STEP IN HISTIDINE BIOSYNTHETIC PATHWAY. IS VERY
IMPORTANT IN THE REGULATION OF HISTIDINE METABOLISM.
SUBUNIT: HOMOHEXAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE ATP PHOSPHORIBOSYLTRANSFERASE FAMILY.
|
| | hisD | b2020 | L-histidinal:NAD+ oxidoreductase; L-histidinol:NAD+ oxidoreductase |
EG10447 |
FUNCTION: THIS PROTEIN IS CONSIDERED AS A BIFUNCTIONAL ENZYME,
POSSESSING TWO ACTIVE SITES, ONE AN ALCOHOL DEHYDROGENASE AND
THE OTHER AN ALDEHYDE DEHYDROGENASE.
CATALYTIC ACTIVITY: L-HISTIDINOL + 2 NAD(+) = L-HISTIDINE +
2 NADH.
PATHWAY: TENTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: HOMODIMER.
SIMILARITY: TO OTHER PROKARYOTIC, FUNGAL AND PLANTS HDH.
|
| | hisC | b2021 | histidinol-phosphate aminotransferase |
EG10446 |
CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + 2-OXOGLUTARATE =
3-(IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + GLUTAMATE.
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: EIGHTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT
AMINOTRANSFERASES.
|
| | hisB | b2022 | imidazoleglycerolphosphate dehydratase and histidinol-phosphate phosphatase |
EG10445 |
CATALYTIC ACTIVITY: D-ERYTHRO-1-(IMIDAZOL-4-YL)GLYCEROL
3-PHOSPHATE = 3-(IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + H(2)O.
CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + H(2)O = L-HISTIDINOL
+ ORTHOPHOSPHATE.
PATHWAY: SEVENTH & NINTH STEPS IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE
IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE FAMILY.
|
| | hisH | b2023 | glutamine amidotransferase subunit of heterodimer with HisF = imidazole glycerol phosphate synthase holoenzyme |
EG10450 |
FUNCTION: CATALYZES AN AMIDOTRANSFERASE REACTION THAT GENERATES
IMIDAZOLE-GLYCEROL PHOSPHATE AND 5-AMINOIMIDAZOL-4-CARBOXAMIDE
RIBONUCLEOTIDE, WHICH IS USED FOR PURINE SYNTHESIS.
PATHWAY: FIFTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE HISH FAMILY.
SIMILARITY: CONTAINS 1 TYPE-1 GLUTAMINE AMIDOTRANSFERASE DOMAIN.
|
| | hisA | b2024 | N-(5'-phospho-L-ribosyl-formimino)-5-amino-1-(5'- phosphoribosyl)-4-imidazolecarboxamide isomerase |
EG10444 |
CATALYTIC ACTIVITY: N-(5'-PHOSPHO-D-RIBOSYLFORMIMINO)-5-AMINO-1-
(5''-PHOSPHORIBOSYL)-4-IMIDAZOLECARBOXAMIDE = N-(5'-PHOSPHO-D-1'-
RIBULOSYLFORMIMINO)-5-AMINO-1-(5''-PHOSPHORIBOSYL)-4-
IMIDAZOLECARBOXAMIDE.
PATHWAY: FOURTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE HISA / HISF FAMILY.
|
| | hisF | b2025 | imidazole glycerol phosphate synthase subunit in heterodimer with HisH = imidazole glycerol phsphate synthase holoenzyme |
EG10448 |
FUNCTION: CATALYZES THE CYCLIZATION REACTION THAT PRODUCES
D-ERYTHRO-IMIDAZOLE GLYCEROL PHOSPHATE.
PATHWAY: SIXTH STEP IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBUNIT: MONOMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE HISA / HISF FAMILY.
|
| | hisI | b2026 | phosphoribosyl-amp cyclohydrolase; phosphoribosyl-ATP pyrophosphatase |
EG10451 |
CATALYTIC ACTIVITY: 5-PHOSPHORIBOSYL-ATP + H(2)O =
5-PHOSPHORIBOSYL-AMP + PYROPHOSPHATE.
CATALYTIC ACTIVITY: 5-PHOSPHORIBOSYL-AMP + H(2)O =
5-(5-PHOSPHO-D-RIBOSYLAMINOFORMIMINO)-1-(5-PHOSPHO-RIBOSYL)
IMIDAZOLE-4-CARBOXAMIDE.
PATHWAY: SECOND AND THIRD STEPS IN HISTIDINE BIOSYNTHETIC PATHWAY.
SUBCELLULAR LOCATION: CYTOPLASMIC.
|
| 0.620879 | - | rsuA | b2183 | 16S pseudouridylate 516 synthase |
EG12044 |
FUNCTION: FORMATION OF PSEUDOURIDINE FROM URACIL-516 IN
16S RIBOSOMAL RNA.
CATALYTIC ACTIVITY: URACIL + D-RIBOSE 5-PHOSPHATE = PSEUDOURIDINE
5'-PHOSPHATE + H(2)O.
SIMILARITY: BELONGS TO FAMILY 1 OF PSEUDOURIDINE SYNTHASES.
FUNCTION: PARTICIPATES IN THE SYNTHESIS OF A MSDNA (A BRANCHED RNA
LINKED BY A 2',5'-PHOSPHODIESTER LINKAGE TO A SINGLE-STRANDED DNA)
OF UNKNOWN FUNCTION. THE RETRON TRANSCRIPT SERVES AS PRIMER AND
TEMPLATE TO THE REACTION, AND CODES FOR THE RT.
CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE =
N PYROPHOSPHATE + DNA(N) (EC 2.7.7.49).
CATALYTIC ACTIVITY: ENDONUCLEOLYTIC CLEAVAGE TO
5'-PHOSPHOMONOESTER (EC 3.1.26.4).
MISCELLANEOUS: RETRONS MAY BE THE ANCESTORS OF RETROVIRUS.
SIMILARITY: TO OTHER REVERSE TRANSCRIPTASES IN BACTERIA AND
RETROVIRUSES.
SIMILARITY: TO OTHER RNASES H ENZYMES OR DOMAINS.
FUNCTION: PARTICIPATES IN THE SYNTHESIS OF A MSDNA (A BRANCHED RNA
LINKED BY A 2',5'-PHOSPHODIESTER LINKAGE TO A SINGLE-STRANDED DNA)
OF UNKNOWN FUNCTION. THE RETRON TRANSCRIPT SERVES AS PRIMER AND
TEMPLATE TO THE REACTION, AND CODES FOR THE RT.
CATALYTIC ACTIVITY: N DEOXYNUCLEOSIDE TRIPHOSPHATE =
N PYROPHOSPHATE + DNA(N).
MISCELLANEOUS: RETRONS MAY BE THE ANCESTORS OF RETROVIRUS.
SIMILARITY: TO OTHER REVERSE TRANSCRIPTASES IN BACTERIA AND
RETROVIRUSES.
|
| | bcr | b2182 | bicyclomycin resistance protein; transmembrane protein |
EG11419 |
FUNCTION: INVOLVED IN SULFONAMIDE (SULFATHIAZOLE) AND
BICYCLOMYCIN RESISTANCE. PROBABLE MEMBRANE TRANSLOCASE.
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE.
SIMILARITY: BELONGS TO THE MAJOR FACILITATOR FAMILY (ALSO KNOWN
AS THE DRUG RESISTANCE TRANSLOCASE FAMILY). BELONGS TO THE
BCR/CMLA SUBFAMILY.
|
| 0.597811 | + | b1995 | b1995 | orf, hypothetical protein |
|
|
| 0.512426 | + | tdcR | b3119 | threonine dehydratase operon activator protein |
EG10992 |
FUNCTION: PROBABLE TRANS-ACTING POSITIVE ACTIVATOR FOR THE TDC
OPERON.
|
| 0.502064 | + | ycjL | b1298 | probable amidotransferase subunit |
EG13909 |
SIMILARITY: TO L.LACTIS HYPOTHETICAL 18.7 KDA PROTEIN IN PEPX
3'REGION (AC P22347).
|
| | ycjC | b1299 | orf, hypothetical protein |
EG12431 |
SIMILARITY: SOME, TO H.INFLUENZAE HI0659.
|
| 0.501695 | + | lpdA | b0116 | lipoamide dehydrogenase (NADH); component of 2-oxodehydrogenase and pyruvate complexes; L-protein of glycine cleavage complex |
EG10543 |
FUNCTION: LIPOAMIDE DEHYDROGENASE IS A COMPONENT OF THE GLYCINE
CLEAVAGE SYSTEM AS WELL AS OF THE ALPHA-KETOACID DEHYDROGENASE
COMPLEXES.
CATALYTIC ACTIVITY: DIHYDROLIPOAMIDE + NAD(+) = LIPOAMIDE + NADH.
COFACTOR: FAD.
SUBUNIT: HOMODIMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND.
SIMILARITY: BELONGS TO THE PYRIDINE NUCLEOTIDE-DISULFIDE
OXIDOREDUCTASES CLASS-I.
|
| 0.480358 | + | ybbX | b0512 | putative hydrolase |
EG13619 |
FUNCTION: INVOLVED IN THE ANAEROBIC UTILIZATION OF ALLANTOIN.
CATALYTIC ACTIVITY: ALLANTOIN + H(2)O = ALLANTOATE.
COFACTOR: ZINC (BY SIMILARITY).
PATHWAY: FIRST STEP IN THE DEGRADATION OF ALLANTOIN (PURINE
CATABOLISM).
INDUCTION: BY GLYOXYLATE.
SIMILARITY: BELONGS TO THE DHOASE FAMILY.
|
| | ybbY | b0513 | putative transport |
EG13620 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
INDUCTION: BY GLYOXYLATE.
SIMILARITY: BELONGS TO THE XANTHINE/URACIL PERMEASES FAMILY.
STRONG, TO B.SUBTILIS YWDJ.
|
| | ybbZ | b0514 | orf, hypothetical protein |
EG13621 |
CATALYTIC ACTIVITY: ATP + (R)-GLYCERATE = ADP + 3-PHOSPHO-(R)-
GLYCERATE.
PATHWAY: GLYOXYLATE CATABOLISM.
INDUCTION: BY GLYOXYLATE.
SIMILARITY: BELONGS TO THE UPF0068 FAMILY.
|
| 0.453113 | + | ybdA | b0591 | putative transport |
EG11104 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
|
| 0.452959 | + | yhiF | b3507 | orf, hypothetical protein |
EG11889 |
SIMILARITY: BELONGS TO THE LUXR/UHPA FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.447040 | + | pheL | b2598 | leader peptide of chorismate mutase-P-prephenate dehydratase |
EG11271 |
FUNCTION: THIS PROTEIN IS INVOLVED IN CONTROL OF THE BIOSYNTHESIS
OF PHENYLALANINE.
|
| | pheA | b2599 | chorismate mutase-P and prephenate dehydratase |
EG10707 |
CATALYTIC ACTIVITY: CHORISMATE = PREPHENATE.
CATALYTIC ACTIVITY: PREPHENATE = PHENYLPYRUVATE + H(2)O + CO(2).
PATHWAY: L-PHENYLALANINE BIOSYNTHESIS.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: TO OTHER PDT ENZYMES OR DOMAINS.
|
| 0.413925 | + | flgG | b1078 | flagellar biosynthesis, cell-distal portion of basal-body rod |
EG14271 |
SUBUNIT: THE BASAL BODY CONSTITUTES A MAJOR PORTION OF THE
FLAGELLAR ORGANELLE AND CONSISTS OF FOUR RINGS (L,P,S, AND M)
MOUNTED ON A CENTRAL ROD. THE ROD CONSISTS OF ABOUT 26 SUBUNITS OF
FLGG IN THE DISTAL PORTION, AND FLGB, FLGC AND FLGF ARE THOUGHT TO
BUILD UP THE PROXIMAL PORTION OF THE ROD WITH ABOUT 6 SUBUNITS
EACH.
SIMILARITY: BELONGS TO THE FLAGELLA BASAL BODY ROD PROTEINS
FAMILY.
|
| | flgH | b1079 | flagellar biosynthesis, basal-body outer-membrane L (lipopolysaccharide layer) ring protein |
EG20264 |
FUNCTION: ASSEMBLES AROUND THE ROD TO FORM THE L-RING AND PROBABLY
PROTECTS THE MOTOR/BASAL BODY FROM SHEARING FORCES DURING
ROTATION.
SUBUNIT: THE BASAL BODY CONSTITUTES A MAJOR PORTION OF THE
FLAGELLAR ORGANELLE AND CONSISTS OF FOUR RINGS (L,P,S, AND M)
MOUNTED ON A CENTRAL ROD.
SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID
ANCHOR (PROBABLE).
SIMILARITY: BELONGS TO THE FLGH FAMILY.
|
| | flgI | b1080 | homolog of Salmonella P-ring of flagella basal body |
EG20265 |
FUNCTION: ASSEMBLES AROUND THE ROD TO FORM THE L-RING AND PROBABLY
PROTECTS THE MOTOR/BASAL BODY FROM SHEARING FORCES DURING
ROTATION.
SUBUNIT: THE BASAL BODY CONSTITUTES A MAJOR PORTION OF THE
FLAGELLAR ORGANELLE AND CONSISTS OF FOUR RINGS (L,P,S, AND M)
MOUNTED ON A CENTRAL ROD.
SUBCELLULAR LOCATION: PERIPLASMIC.
SIMILARITY: BELONGS TO THE FLGI FAMILY.
|
| | flgJ | b1081 | flagellar biosynthesis |
EG14272 |
FUNCTION: NOT KNOWN.
|
| | flgK | b1082 | flagellar biosynthesis, hook-filament junction protein 1 |
EG11967 |
SIMILARITY: BELONGS TO THE FLAGELLA BASAL BODY ROD PROTEINS
FAMILY.
|
| | flgL | b1083 | flagellar biosynthesis; hook-filament junction protein |
EG11545 |
SIMILARITY: BELONGS TO THE BACTERIAL FLAGELLIN FAMILY.
|
| 0.384700 | - | ybjX | b0877 | putative enzyme |
EG13693 |
SIMILARITY: TO H.INFLUENZAE HI0461 AND WEAK, TO P.HAEMOLYTICA
LAPB.
|
| 0.367757 | + | metB | b3939 | cystathionine gamma-synthase |
EG10582 |
CATALYTIC ACTIVITY: O-SUCCINYL-L-HOMOSERINE + L-CYSTEINE =
CYSTATHIONINE + SUCCINATE (CAN ALSO USE HYDROGEN SULFIDE AND
METHANETHIOL AS SUBSTRATES).
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: SECOND STEP IN METHIONINE BIOSYNTHESIS.
SUBUNIT: HOMOTETRAMER.
SUBCELLULAR LOCATION: CYTOPLASMIC.
SIMILARITY: BELONGS TO THE TRANS-SULFURATION ENZYMES FAMILY.
|
| | metL | b3940 | aspartokinase II and homoserine dehydrogenase II |
EG10590 |
CATALYTIC ACTIVITY: L-HOMOSERINE + NAD(P)(+) = L-ASPARTATE
BETA-SEMIALDEHYDE + NAD(P)H.
CATALYTIC ACTIVITY: ATP + L-ASPARTATE = ADP + 4-PHOSPHO-L-
ASPARTATE.
PATHWAY: CATALYZES 2 NONCONSECUTIVE REACTIONS IN THE COMMON
BIOSYNTHETIC PATHWAY LEADING FROM ASP TO DIAMINOPIMELATE AND LYS,
TO MET, AND TO THR AND ILE.
SUBUNIT: HOMOTETRAMER.
MISCELLANEOUS: ASPARTOKINASE I-HOMOSERINE DEHYDROGENASE I AND
ASPARTOKINASE III ALSO CATALYZE THE SAME REACTION(S).
SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE
ASPARTOKINASE FAMILY.
SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE
HOMOSERINE DEHYDROGENASE FAMILY.
|
| 0.360029 | + | yidL | b3680 | putative ARAC-type regulatory protein |
EG11707 |
SIMILARITY: BELONGS TO THE ARAC/XYLS FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| 0.355082 | + | add | b1623 | adenosine deaminase |
EG10030 |
CATALYTIC ACTIVITY: ADENOSINE + H(2)O = INOSINE + NH(3) (ALSO ACTS
ON DEOXYADENOSINE).
SIMILARITY: BELONGS TO THE ADENOSINE AND AMP DEAMINASES FAMILY.
|
| 0.348222 | - | b1057 | b1057 | putative cytochrome |
EG12659 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (POTENTIAL).
SIMILARITY: BELONGS TO THE CYTOCHROME B561 FAMILY.
|
| | yceI | b1056 | orf, hypothetical protein |
EG11820 |
SUBCELLULAR LOCATION: PERIPLASMIC (POTENTIAL).
|
| 0.336775 | + | b2833 | b2833 | orf, hypothetical protein |
EG13076 |
SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID
ANCHOR (POTENTIAL).
SIMILARITY: STRONG, TO E.COLI YGDI.
|
| | b2834 | b2834 | orf, hypothetical protein |
EG13093 |
SIMILARITY: BELONGS TO THE ALDO/KETO REDUCTASE 2 FAMILY.
|
| 0.331744 | + | chaB | b1217 | cation transport regulator |
EG12402 |
|
| | chaC | b1218 | cation transport regulator |
EG12403 |
|
| 0.328376 | + | sodA | b3908 | superoxide dismutase, manganese |
EG10953 |
FUNCTION: DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE
CELLS AND ARE TOXIC TO BIOLOGICAL SYSTEMS.
CATALYTIC ACTIVITY: 2 PEROXIDE RADICAL + 2 H(+) = O(2) + H(2)O(2).
SUBUNIT: HOMODIMER.
SIMILARITY: BELONGS TO THE IRON/MANGANESE SUPEROXIDE DISMUTASE
FAMILY.
|
| 0.320156 | - | rpsJ | b3321 | 30S ribosomal subunit protein S10 |
EG10909 |
FUNCTION: THIS PROTEIN IS INVOLVED IN THE BINDING OF TRNA TO THE
RIBOSOMES.
MASS SPECTROMETRY: MW=11734.5; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S10P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplC | b3320 | 50S ribosomal subunit protein L3 |
EG10866 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY TO 23S RIBOSOMAL RNA AND MAY
PARTICIPATE IN THE FORMATION OF THE PEPTIDYLTRANSFERASE CENTER OF
THE RIBOSOME.
MASS SPECTROMETRY: MW=22257.2; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L3P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplD | b3319 | 50S ribosomal subunit protein L4, regulates expression of S10 operon |
EG10867 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY AND SPECIFICALLY TO 23S
RRNA.
FUNCTION: PROTEIN L4 IS ALSO A TRANSLATIONAL REPRESSOR PROTEIN, IT
CONTROLS THE TRANSLATION OF THE S10 OPERON (TO WHICH BELONG L4) BY
BINDING TO ITS MRNA.
MASS SPECTROMETRY: MW=22086.2; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L4P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplW | b3318 | 50S ribosomal subunit protein L23 |
EG10883 |
FUNCTION: BINDS TO A SPECIFIC REGION ON THE 23S RRNA.
MASS SPECTROMETRY: MW=11198.0; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L23P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplB | b3317 | 50S ribosomal subunit protein L2 |
EG10865 |
FUNCTION: THIS PROTEIN IS A PRIMARY 23S RRNA-BINDING PROTEIN. IT
HAS PEPTIDYLTRANSFERASE ACTIVITY.
MASS SPECTROMETRY: MW=29732.3; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L2P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsS | b3316 | 30S ribosomal subunit protein S19 |
EG10918 |
FUNCTION: PROTEIN S19 FORMS A COMPLEX WITH S13 THAT BINDS STRONGLY
TO THE 16S RIBOSOMAL RNA.
MASS SPECTROMETRY: MW=10299.6; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S19P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rplV | b3315 | 50S ribosomal subunit protein L22 |
EG10882 |
FUNCTION: THIS PROTEIN BINDS SPECIFICALLY TO 23S RRNA; ITS BINDING
IS STIMULATED BY OTHER RIBOSOMAL PROTEINS, E.G., L4, L17, AND L20.
IT IS IMPORTANT DURING THE EARLY STAGES OF 50S RECONSTITUTION.
MASS SPECTROMETRY: MW=12225.3; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L22P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpsC | b3314 | 30S ribosomal subunit protein S3 |
EG10902 |
FUNCTION: THIS PROTEIN IS INVOLVED IN THE BINDING OF INITIATOR
MET-TRNA.
MASS SPECTROMETRY: MW=25851.9; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S3P FAMILY OF RIBOSOMAL PROTEINS.
SIMILARITY: CONTAINS 1 KH DOMAIN.
|
| | rplP | b3313 | 50S ribosomal subunit protein L16 |
EG10877 |
FUNCTION: THIS PROTEIN BINDS DIRECTLY TO 23S RIBOSOMAL RNA AND IS
LOCATED AT THE A SITE OF THE PEPTIDYLTRANSFERASE CENTER.
MASS SPECTROMETRY: MW=15326.2; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L16P FAMILY OF RIBOSOMAL PROTEINS.
|
| | rpmC | b3312 | 50S ribosomal subunit protein L29 |
EG10887 |
MASS SPECTROMETRY: MW=7273.4; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L29P FAMILY OF RIBOSOMAL PROTEINS.
CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO AN EXCHANGE
OF TWO TRYPTIC PEPTIDES.
|
| | rpsQ | b3311 | 30S ribosomal subunit protein S17 |
EG10916 |
FUNCTION: PROTEIN S17 BINDS SPECIFICALLY TO THE 5' END OF 16S
RIBOSOMAL RNA. S17 IS THOUGHT TO BE INVOLVED IN THE RECOGNITION OF
TERMINATION CODONS.
MASS SPECTROMETRY: MW=9573.0; METHOD=MALDI.
SIMILARITY: BELONGS TO THE S17P FAMILY OF RIBOSOMAL PROTEINS.
|
| 0.316041 | + | ebgR | b3075 | regulator of ebg operon |
EG10254 |
FUNCTION: REPRESSOR FOR BETA GALACTOSIDASE ALPHA AND BETA
SUBUNITS (EBGA AND EBGC). BINDS LACTOSE AS AN INDUCER.
SIMILARITY: BELONGS TO THE LACI FAMILY OF TRANSCRIPTIONAL
REGULATORS.
|
| | ebgA | b3076 | evolved beta-D-galactosidase, alpha subunit; cryptic gene |
EG10252 |
FUNCTION: THE WILD-TYPE ENZYME IS AN INEFFECTIVE LACTASE. TWO
CLASSES OF POINT MUTATIONS DRAMATICALLY IMPROVE ACTIVITY OF THE
ENZYME.
CATALYTIC ACTIVITY: HYDROLYSIS OF TERMINAL, NON-REDUCING BETA-D-
GALACTOSE RESIDUES IN BETA-D-GALACTOSIDES.
SUBUNIT: HETEROOCTAMER OF 4 ALPHA AND 4 BETA SUBUNITS.
SIMILARITY: BELONGS TO FAMILY 2 OF GLYCOSYL HYDROLASES.
|
| | ebgC | b3077 | evolved beta-D-galactosidase, beta subunit; cryptic gene |
EG10253 |
FUNCTION: REQUIRED FOR FULL ACTIVITY OF THE EBGA ENZYME. EXACT
FUNCTION NOT KNOWN.
SUBUNIT: HETEROOCTAMER OF 4 ALPHA AND 4 BETA SUBUNITS.
|
| | ygjI | b3078 | putative oxidoreductase |
EG12720 |
SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN. INNER MEMBRANE
(POTENTIAL).
SIMILARITY: BELONGS TO THE XASA FAMILY OF TRANSPORTERS.
|
| | ygjJ | b3079 | orf, hypothetical protein |
EG12721 |
|
| | ygjK | b3080 | putative isomerase |
EG12722 |
|
| 0.299426 | - | lysA | b2838 | diaminopimelate decarboxylase |
EG10549 |
CATALYTIC ACTIVITY: MESO-2,6-DIAMINOHEPTANEDIOATE = L-LYSINE +
CO(2).
COFACTOR: PYRIDOXAL PHOSPHATE.
PATHWAY: LAST STEP IN THE BIOSYNTHESIS OF LYSINE.
SIMILARITY: BELONGS TO FAMILY 2 OF ORNITHINE, DAP, AND ARGININE
DECARBOXYLASES.
|
| 0.298987 | + | aroH | b1704 | 3-deoxy-D-arabinoheptulosonate-7-phosphate synthase (DAHP synthetase, tryptophan repressible) |
EG10080 |
FUNCTION: STEREOSPECIFIC CONDENSATION OF PHOSPHOENOLPYRUVATE (PEP)
AND D-ERYTHROSE-4-PHOSPHATE (E4P) GIVING RISE TO 3-DEOXY-D-
ARABINO-HEPTULOSONATE-7-PHOSPHATE (DAHP).
CATALYTIC ACTIVITY: 7-PHOSPHO-2-DEHYDRO-3-DEOXY-D-ARABINO-
HEPTONATE + ORTHOPHOSPHATE = PHOSPHOENOLPYRUVATE + D-ERYTHROSE
4-PHOSPHATE + H(2)O.
PATHWAY: FIRST STEP IN THE BIOSYNTHESIS OF CHORISMATE WITHIN
THE BIOSYNTHESIS OF AROMATIC AMINO ACIDS (THE SHIKIMATE PATHWAY).
MISCELLANEOUS: THERE ARE 3 DAHP SYNTHASES, AROH IS
FEEDBACK-INHIBITED BY TRP. THE OTHER 2 DAHP SYNTHASES ARE TYR- AND
PHE-SENSITIVE, RESPECTIVELY.
SIMILARITY: BELONGS TO CLASS-I DAHP SYNTHETASE FAMILY.
|
| | ydiE | b1705 | orf, hypothetical protein |
EG12391 |
SIMILARITY: TO Y.ENTEROCOLITICA HEMP.
|
| 0.295069 | - | b2971 | b2971 | orf, hypothetical protein |
EG12991 |
SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID
ANCHOR (POTENTIAL).
|
| | b2970 | b2970 | putative general secretion pathway for protein export (GSP) |
EG12990 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: PERIPLASMIC (POTENTIAL).
SIMILARITY: BELONGS TO THE EXEC/PULC/OUTC FAMILY.
|
| | yghE | b2969 | putative general secretion pathway for protein export (GSP) |
EG12989 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: INNER MEMBRANE (PROBABLE).
SIMILARITY: BELONGS TO THE EXEL/PULL/OUTL/XCPY FAMILY.
|
| | yghD | b2968 | putative secretion pathway protein |
EG12988 |
FUNCTION: INVOLVED IN A GENERAL SECRETION PATHWAY (GSP) FOR THE
EXPORT OF PROTEINS (BY SIMILARITY).
SUBCELLULAR LOCATION: INNER MEMBRANE (PROBABLE).
SIMILARITY: BELONGS TO THE EXEM/PULM/OUTM/XCPZ FAMILY.
|
| 0.286774 | + | htpG | b0473 | chaperone Hsp90, heat shock protein C 62.5 |
EG10461 |
FUNCTION: MOLECULAR CHAPERONE. HAS ATPASE ACTIVITY.
SIMILARITY: BELONGS TO THE HEAT SHOCK PROTEIN 90 FAMILY.
|
| 0.281906 | + | b2443 | b2443 | orf, hypothetical protein |
EG14173 |
|
| 0.265675 | + | yejH | b2184 | putative ATP-dependent helicase |
EG12045 |
SIMILARITY: SOME SIMILARITY TO A PHAGE PROTEIN AND RESTRICTION-
MODIFICATION SYSTEMS.
CAUTION: REF.1 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO FRAMESHIFTS
THAT PRODUCE THREE SEPARATE ORFS.
|
| | rplY | b2185 | 50S ribosomal subunit protein L25 |
EG10885 |
FUNCTION: BINDS TO THE 5S RRNA.
MASS SPECTROMETRY: MW=10693.4; METHOD=MALDI.
SIMILARITY: BELONGS TO THE L25P FAMILY OF RIBOSOMAL PROTEINS.
|
| 0.262686 | + | htrA | b0161 | periplasmic serine protease Do; heat shock protein HtrA |
EG10463 |
FUNCTION: SERINE PROTEASE THAT IS REQUIRED AT HIGH TEMPERATURE.
INVOLVED IN THE DEGRADATION OF DAMAGED PROTEINS. IT CAN DEGRADES
ICIA, ADA, CASEIN AND GLOBIN. SHARED SPECIFICITY WITH DEGQ.
SUBUNIT: MULTIMERIC.
SUBCELLULAR LOCATION: PERIPLASMIC.
INDUCTION: HEAT SHOCK.
MISCELLANEOUS: HTRA IS INDISPENSABLE FOR BACTERIAL SURVIVAL AT
TEMPERATURES ABOVE 42 DEGREES CELSIUS.
SIMILARITY: BELONGS TO PEPTIDASE FAMILY S2C; ALSO KNOWN AS THE
DEGP/DEGQ/DEGS FAMILY.
SIMILARITY: CONTAINS 2 PDZ/DHR DOMAINS.
|
| | yaeG | b0162 | orf, hypothetical protein |
EG12335 |
FUNCTION: SEEMS TO REGULATE THE EXPRESSION OF THE OPERONS FOR THE
ENZYMES INVOLVED IN D-GALACTARATE, D-GLUCARATE AND D-GLYCERATE
UTILIZATION.
SIMILARITY: BELONGS TO THE CDAR FAMILY.
|