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Database: UniProt
Entry: VIBB_VIBC3
LinkDB: VIBB_VIBC3
Original site: VIBB_VIBC3 
ID   VIBB_VIBC3              Reviewed;         293 AA.
AC   A5F3F4; C3LYD9; O07900; Q9JQ11;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Vibriobactin-specific isochorismatase;
DE            EC=3.3.2.1;
DE   AltName: Full=2,3 dihydro-2,3 dihydroxybenzoate synthase;
DE   AltName: Full=Isochorismate lyase-ArCP;
GN   Name=vibB; OrderedLocusNames=VC0395_A0300, VC395_0788;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11112537; DOI=10.1021/bi001651a;
RA   Keating T.A., Marshall C.G., Walsh C.T.;
RT   "Vibriobactin biosynthesis in Vibrio cholerae: VibH is an amide synthase
RT   homologous to nonribosomal peptide synthetase condensation domains.";
RL   Biochemistry 39:15513-15521(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of the catechol siderophore
CC       vibriobactin. Vibriobactin is a chelating compound involved in
CC       transporting iron from the bacterial environment into the cell
CC       cytoplasm (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + isochorismate = (2S,3S)-2,3-dihydroxy-2,3-
CC         dihydrobenzoate + pyruvate; Xref=Rhea:RHEA:11112, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29780, ChEBI:CHEBI:58764; EC=3.3.2.1;
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC   -!- PATHWAY: Siderophore biosynthesis; vibriobactin biosynthesis.
CC   -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR   EMBL; AF287252; AAG00563.1; -; Genomic_DNA.
DR   EMBL; CP000627; ABQ20715.1; -; Genomic_DNA.
DR   EMBL; CP001235; ACP08805.1; -; Genomic_DNA.
DR   RefSeq; WP_000997093.1; NZ_JAACZH010000017.1.
DR   AlphaFoldDB; A5F3F4; -.
DR   SMR; A5F3F4; -.
DR   KEGG; vco:VC0395_A0300; -.
DR   KEGG; vcr:VC395_0788; -.
DR   PATRIC; fig|345073.21.peg.762; -.
DR   eggNOG; COG1535; Bacteria.
DR   eggNOG; COG3433; Bacteria.
DR   HOGENOM; CLU_068979_2_0_6; -.
DR   OrthoDB; 5794853at2; -.
DR   UniPathway; UPA00022; -.
DR   Proteomes; UP000000249; Chromosome 2.
DR   GO; GO:0008908; F:isochorismatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019537; P:vibriobactin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01013; isochorismatase; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.850; Isochorismatase-like; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR016291; Isochorismatase.
DR   InterPro; IPR000868; Isochorismatase-like.
DR   InterPro; IPR036380; Isochorismatase-like_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR43540:SF3; ENTEROBACTIN SYNTHASE COMPONENT B; 1.
DR   PANTHER; PTHR43540; PEROXYUREIDOACRYLATE/UREIDOACRYLATE AMIDOHYDROLASE-RELATED; 1.
DR   Pfam; PF00857; Isochorismatase; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001111; Isochorismatase; 1.
DR   PRINTS; PR01398; ISCHRISMTASE.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52499; Isochorismatase-like hydrolases; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Phosphopantetheine; Phosphoprotein.
FT   CHAIN           1..293
FT                   /note="Vibriobactin-specific isochorismatase"
FT                   /id="PRO_0000321856"
FT   DOMAIN          211..287
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         248
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   293 AA;  32553 MW;  A64283991E17A3F5 CRC64;
     MAIPKIASYP LPVSLPTNKV DWRIDASRAV LLIHDMQEYF VHYFDSQAEP IPSLIKHIQQ
     LKAHAKQAGI PVVYTAQPAN QDPAERALLS DFWGPGLSEE TAIIAPLAPE SGDVQLTKWR
     YSAFKKSPLL DWLRETGRDQ LIITGVYAHI GILSTALDAF MFDIQPFVIG DGVADFSLSD
     HEFSLRYISG RTGAVKSTQQ ACLEIAAQHS KLTGLSLRTM QHDVAAALNL SVDEVDVQEN
     LLFLGLDSIR AIQLLEKWKA QGADISFAQL MEHVTLQQWW QTIQANLHQP CSA
//
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