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
//