ID   VIBA_VIBCH              Reviewed;         262 AA.
AC   Q56632; Q9JQ08;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Vibriobactin-specific 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase;
DE            EC=1.3.1.28;
GN   Name=vibA; OrderedLocusNames=VC_0774;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor Lou15;
RX   PubMed=9371453; DOI=10.1128/jb.179.22.7055-7062.1997;
RA   Wyckoff E.E., Stoebner J.A., Reed K.E., Payne S.M.;
RT   "Cloning of a Vibrio cholerae vibriobactin gene cluster: identification of
RT   genes required for early steps in siderophore biosynthesis.";
RL   J. Bacteriol. 179:7055-7062(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Involved in an early step of the biosynthesis of the catechol
CC       siderophore vibriobactin. Vibriobactin is a chelating compound involved
CC       in transporting iron from the bacterial environment into the cell
CC       cytoplasm.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD(+) = 2,3-
CC         dihydroxybenzoate + H(+) + NADH; Xref=Rhea:RHEA:23824,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:36654, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58764; EC=1.3.1.28;
CC   -!- PATHWAY: Siderophore biosynthesis; vibriobactin biosynthesis.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; U52150; AAC45924.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF93939.1; -; Genomic_DNA.
DR   PIR; G82280; G82280.
DR   RefSeq; NP_230423.1; NC_002505.1.
DR   RefSeq; WP_000654285.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q56632; -.
DR   SMR; Q56632; -.
DR   STRING; 243277.VC_0774; -.
DR   DNASU; 2615317; -.
DR   EnsemblBacteria; AAF93939; AAF93939; VC_0774.
DR   GeneID; 57739484; -.
DR   KEGG; vch:VC_0774; -.
DR   PATRIC; fig|243277.26.peg.738; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_0_6; -.
DR   OMA; MHDLYVD; -.
DR   BioCyc; MetaCyc:VC0774-MON; -.
DR   BioCyc; VCHO:VC0774-MON; -.
DR   UniPathway; UPA00022; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0008667; F:2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR   GO; GO:0019537; P:vibriobactin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05331; DH-DHB-DH_SDR_c; 1.
DR   InterPro; IPR003560; DHB_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   PRINTS; PR01397; DHBDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR04316; dhbA_paeA; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..262
FT                   /note="Vibriobactin-specific 2,3-dihydro-2,3-
FT                   dihydroxybenzoate dehydrogenase"
FT                   /id="PRO_0000054808"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         12..36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  28093 MW;  977C9CB943E800CD CRC64;
     MKDMSLVNSK VLLVGSARGI GFSVLEHLLQ AGAQVMAADC EWQLLLEQSE SLLGRYPDQL
     TLKKLDLAEP EAVREQVNQW AEQVAGFDHL VCCAGILHVA PLHEMPMEQV SSIFTVNAFG
     VLACMQGVAS SMKARQQGSM VIIGSNAANT PRMSIGAYGA SKAALHMLVK CIGMELAPYG
     IRCNLVSPGS TRTAMQQQLW TEQYGEAQVI AGDAAQFRLG IPLNKIAEPA DIAQAVLFLL
     SDNAGHITLH DLRVDGGATL DH