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Database: UniProt
Entry: C9P5K0_VIBME
LinkDB: C9P5K0_VIBME
Original site: C9P5K0_VIBME 
ID   C9P5K0_VIBME            Unreviewed;       329 AA.
AC   C9P5K0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE            Short=OSB synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE            Short=OSBS {ECO:0000256|HAMAP-Rule:MF_00470};
DE            EC=4.2.1.113 {ECO:0000256|HAMAP-Rule:MF_00470};
DE   AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE   AltName: Full=o-succinylbenzoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00470};
GN   Name=menC {ECO:0000256|HAMAP-Rule:MF_00470};
GN   ORFNames=VIB_001579 {ECO:0000313|EMBL:EEX37454.1};
OS   Vibrio metschnikovii CIP 69.14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX37454.1, ECO:0000313|Proteomes:UP000005604};
RN   [1] {ECO:0000313|EMBL:EEX37454.1, ECO:0000313|Proteomes:UP000005604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX37454.1,
RC   ECO:0000313|Proteomes:UP000005604};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA   Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA   Vonstein V.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC       carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000256|HAMAP-
CC       Rule:MF_00470}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate
CC         = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00470};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00470};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
CC       {ECO:0000256|HAMAP-Rule:MF_00470}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00470}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. MenC type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00470}.
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DR   EMBL; ACZO01000006; EEX37454.1; -; Genomic_DNA.
DR   RefSeq; WP_004395556.1; NZ_ACZO01000006.1.
DR   AlphaFoldDB; C9P5K0; -.
DR   STRING; 675813.VIB_001579; -.
DR   GeneID; 79887457; -.
DR   eggNOG; COG1441; Bacteria.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000005604; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03320; OSBS; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   HAMAP; MF_00470; MenC_1; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR048639; MenC_N.
DR   InterPro; IPR010196; OSB_synthase_MenC1.
DR   NCBIfam; TIGR01927; menC_gam_Gplu; 1.
DR   PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR   Pfam; PF21508; MenC_N; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00009; o-succinylbenzoate_synthase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00470};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00470};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00470};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00470}; Reference proteome {ECO:0000313|Proteomes:UP000005604}.
FT   DOMAIN          116..213
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        135
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   ACT_SITE        241
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         163
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ   SEQUENCE   329 AA;  35912 MW;  592091A0C41344E5 CRC64;
     MRSAKLYQYQ LPMDSGVILR DQKLTQREGF IVELEQDGQI GRGEIAPLIG FSRESLQEAG
     ALAKEQLALW VQGKEVQIGN DFPSVAFGLS MAQMELAGEL SSEGQYHCAP LCSGDPDELI
     PLLNAMPGQK VAKVKVGLYE PIRDGMLVNL FLESMPDLQL RLDANQAWSK EKAAKFSQYV
     SPSVRGRIAF LEEPCRSPSD SLAFAIDSGI AIAWDETLQH AVQQADFQLE DLTGAKAIVI
     KPTLIGSVQT CQALIEKARS LGIQAVISSS LESSLGLTQL ARLSHWLLPE TIPGLDTIGL
     FKAQLETPWP GCTLPVHTLD QQTLVWQSA
//
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