VENB_VIBVU
ID VENB_VIBVU Reviewed; 295 AA.
AC P74965;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Probable isochorismatase;
DE EC=3.3.2.1;
DE AltName: Full=2,3 dihydro-2,3 dihydroxybenzoate synthase;
GN Name=venB; OrderedLocusNames=VV2_0838;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MO6-24;
RX PubMed=8698519; DOI=10.1128/iai.64.7.2834-2838.1996;
RA Litwin C.M., Rayback T.W., Skinner J.;
RT "Role of catechol siderophore synthesis in Vibrio vulnificus virulence.";
RL Infect. Immun. 64:2834-2838(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of the catechol siderophore
CC vulnibactin. Vulnibactin 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; vulnibactin biosynthesis.
CC -!- SIMILARITY: Belongs to the isochorismatase family. {ECO:0000305}.
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DR EMBL; U32676; AAB18150.1; -; Genomic_DNA.
DR EMBL; AE016796; AAO07761.1; -; Genomic_DNA.
DR RefSeq; WP_011081755.1; NC_004460.2.
DR AlphaFoldDB; P74965; -.
DR SMR; P74965; -.
DR EnsemblBacteria; AAO07761; AAO07761; VV2_0838.
DR KEGG; vvu:VV2_0838; -.
DR HOGENOM; CLU_068979_2_0_6; -.
DR OMA; RDIKPFF; -.
DR UniPathway; UPA00021; -.
DR Proteomes; UP000002275; Chromosome 2.
DR GO; GO:0008908; F:isochorismatase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Hydrolase; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..295
FT /note="Probable isochorismatase"
FT /id="PRO_0000201828"
FT DOMAIN 207..286
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 115
FT /note="G -> D (in Ref. 1; AAB18150)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="E -> Q (in Ref. 1; AAB18150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 33205 MW; 2062BA63CD8CB0CC CRC64;
MGIPKIAGYP LPTPAEFPDN RTGWTIDPDQ AVLLIHDMQE YFVNYYQPDS SPVVDIIQHI
QRLKAAAKKA GIPVIYTAQP ANQHPTDRAL LTDFWGPGLN GDHVPIVEAL SPEEGDIEYV
KWRYSAFKKT PLLEFMRAQG KSQLIISGIY GHIGILSTTL DAFMLDIQPF VIGDAIADFT
REDHLRTLEY VASRSGSVKR LDEALDEIRS QKPLTLEQIQ QDVATSLGIQ PDEVDLDEDL
MFVGLDSMRA MVLVEKWHQQ GENISFGQLM EAASLREWWL VIEQARNEEQ TMAVA