VIBB_VIBCH
ID VIBB_VIBCH Reviewed; 293 AA.
AC P0C6D3; O07900; Q9JQ11;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=VC_0771;
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 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.
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; U52150; AAC45926.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF93936.1; -; Genomic_DNA.
DR PIR; G82282; G82282.
DR RefSeq; NP_230420.1; NC_002505.1.
DR RefSeq; WP_000997093.1; NZ_LT906614.1.
DR PDB; 3TB4; X-ray; 1.35 A; A=1-215.
DR PDB; 3TG2; X-ray; 1.10 A; A=1-215.
DR PDBsum; 3TB4; -.
DR PDBsum; 3TG2; -.
DR AlphaFoldDB; P0C6D3; -.
DR SMR; P0C6D3; -.
DR STRING; 243277.VC_0771; -.
DR DNASU; 2615314; -.
DR EnsemblBacteria; AAF93936; AAF93936; VC_0771.
DR GeneID; 57739481; -.
DR KEGG; vch:VC_0771; -.
DR PATRIC; fig|243277.26.peg.735; -.
DR eggNOG; COG1535; Bacteria.
DR eggNOG; COG3433; Bacteria.
DR HOGENOM; CLU_068979_2_0_6; -.
DR OMA; RDIKPFF; -.
DR BioCyc; MetaCyc:VC0771-MON; -.
DR BioCyc; VCHO:VC0771-MON; -.
DR BRENDA; 3.3.2.1; 6626.
DR UniPathway; UPA00022; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0008908; F:isochorismatase activity; IEA:UniProtKB-EC.
DR GO; GO:0019537; P:vibriobactin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.40.50.850; -; 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 Pfam; PF00857; Isochorismatase; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001111; Isochorismatase; 1.
DR PRINTS; PR01398; ISCHRISMTASE.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52499; SSF52499; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..293
FT /note="Vibriobactin-specific isochorismatase"
FT /id="PRO_0000201827"
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"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:3TG2"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:3TG2"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3TG2"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3TG2"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3TG2"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:3TG2"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3TG2"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3TG2"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:3TG2"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3TG2"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:3TG2"
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
