Reviewed,
UniProtKB/Swiss-Prot P15047 (ENTA_ECOLI)
Last modified
June 16, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase EC=1.3.1.28 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 248 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 2,3-dihydro-2,3-dihydroxybenzoate + NAD+ = 2,3-dihydroxybenzoate + NADH. |
| Pathway | |
| Subunit structure | Homooctamer. |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Enterobactin biosynthesis Ion transport Iron transport Transport |
| Ligand | Iron NAD |
| Molecular function | Oxidoreductase |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | enterobactin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW iron ion transportInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity Inferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 248 | 248 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase | PRO_0000054659 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 9 – 33 | 25 | NAD By similarity | ||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||
| Active site | 144 | 1 | Proton acceptor By similarity | ||||||||||||||||||||||||||||||||||||||||
| Binding site | 131 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 7 – 12 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 16 – 27 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 31 – 37 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 45 – 50 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 56 – 69 | 14 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 75 – 78 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 88 – 90 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 103 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 105 – 121 | 17 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 125 – 129 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 132 – 134 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 162 | 21 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 163 – 165 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 168 – 174 | 7 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 215 – 226 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 228 – 230 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 237 – 241 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 242 – 247 | 6 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase." Liu J., Duncan K., Walsh C.T. J. Bacteriol. 171:791-798(1989) [PubMed: 2521622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14. |
| [2] | "Nucleotide sequence and transcriptional organization of the Escherichia coli enterobactin biosynthesis cistrons entB and entA." Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A. J. Bacteriol. 171:784-790(1989) [PubMed: 2521621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [5] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M24148 Unassigned DNA. Translation: AAA16103.1. M24143 Genomic DNA. Translation: AAA76836.1. U82598 Genomic DNA. Translation: AAB40796.1. Different initiation. U00096 Genomic DNA. Translation: AAC73697.1. AP009048 Genomic DNA. Translation: BAE76351.1. | |||||||||||||
| PIR | DEECDB. A91904. | ||||||||||||
| RefSeq | AP_001243.1. NP_415128.1. | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| DIP | DIP:9511N. | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 945284. | ||||||||||||
| GenomeReviews | Gene locus JW0588 in contig AP009048_GR. Gene locus b0596 in contig U00096_GR. | ||||||||||||
| KEGG | ecj:JW0588. eco:b0596. | ||||||||||||
Organism-specific databases | |||||||||||||
| EchoBASE | EB0255. | ||||||||||||
| EcoGene | EG10259. entA. | ||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P15047. | ||||||||||||
| OMA | P15047. HASHITL. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | EcoCyc:ENTA-MON. MetaCyc:ENTA-MON. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR002198. DH_sc/Rdtase_SDR. IPR003560. DHB_DH. IPR016040. NAD(P)-bd_dom. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. | ||||||||||||
| PANTHER | PTHR19410. ADH_short_C2. 1 hit. | ||||||||||||
| Pfam | PF00106. adh_short. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR01397. DHBDHDRGNASE. PR00080. SDRFAMILY. | ||||||||||||
| PROSITE | PS00061. ADH_SHORT. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | ENTA_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P15047 Secondary accession number(s): P77100, Q2MBK5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


