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Database: UniProt
Entry: B0JIV6_MICAN
LinkDB: B0JIV6_MICAN
Original site: B0JIV6_MICAN 
ID   B0JIV6_MICAN            Unreviewed;       321 AA.
AC   B0JIV6;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   24-JAN-2024, entry version 90.
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   OrderedLocusNames=MAE_58420 {ECO:0000313|EMBL:BAG05664.1};
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG05664.1, ECO:0000313|Proteomes:UP000001510};
RN   [1] {ECO:0000313|EMBL:BAG05664.1, ECO:0000313|Proteomes:UP000001510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 {ECO:0000313|EMBL:BAG05664.1,
RC   ECO:0000313|Proteomes:UP000001510};
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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: Cofactor biosynthesis; phylloquinone biosynthesis.
CC       {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   -!- 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; AP009552; BAG05664.1; -; Genomic_DNA.
DR   RefSeq; WP_012268043.1; NC_010296.1.
DR   AlphaFoldDB; B0JIV6; -.
DR   STRING; 449447.MAE_58420; -.
DR   PaxDb; 449447-MAE_58420; -.
DR   EnsemblBacteria; BAG05664; BAG05664; MAE_58420.
DR   KEGG; mar:MAE_58420; -.
DR   PATRIC; fig|449447.4.peg.5348; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_030273_0_2_3; -.
DR   OMA; TFKWKIG; -.
DR   BioCyc; MAER449447:MAE_RS25485-MONOMER; -.
DR   UniPathway; UPA00995; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000001510; Chromosome.
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:InterPro.
DR   GO; GO:0042372; P:phylloquinone 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; 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   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|HAMAP-Rule:MF_00470};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00470};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00470}.
FT   DOMAIN          23..94
FT                   /note="MenC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21508"
FT   DOMAIN          133..257
FT                   /note="Enolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13378"
FT   ACT_SITE        140
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   ACT_SITE        245
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         169
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ   SEQUENCE   321 AA;  36856 MW;  C24C890847EEA7F7 CRC64;
     MYFWQFRVYQ RPLLHPLQTH HGLWQIREGI IIRLEAEDGR IGWGEIAPLP EFGSETLSAA
     ILFCQSLENP LSINSIFSIP EQFPACQFAF ESALEDLSIE NKSRELEPRN YSYLLPTGAA
     VFPCLDDILA TNQTNTYKWK IAVNSLPQEL KLFEKLITRL PRNIKLRLDA NGGLSIADSK
     IWLKIADESK IIEFIEQPLP PSQWLEMLQL SQDFTTGIAL DESVANLRQI EECYQRGWRG
     IFVIKPAITG SIQGLRNLWK KYPLDLVFSS VLETNIGRKS ALRLAQEYPK KERALGFGVQ
     QWFNNSDPDW LEKLWTTSAN N
//
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