MENC_SHIFL
ID MENC_SHIFL Reviewed; 320 AA.
AC Q83QT6; Q7C0R1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_00470};
DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_00470};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00470};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00470};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_00470};
GN OrderedLocusNames=SF2340, S2474;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00470};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_00470}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00470}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00470}.
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DR EMBL; AE005674; AAN43854.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17673.1; -; Genomic_DNA.
DR RefSeq; NP_708147.1; NC_004337.2.
DR RefSeq; WP_001255584.1; NZ_WPGW01000032.1.
DR AlphaFoldDB; Q83QT6; -.
DR SMR; Q83QT6; -.
DR STRING; 198214.SF2340; -.
DR EnsemblBacteria; AAN43854; AAN43854; SF2340.
DR EnsemblBacteria; AAP17673; AAP17673; S2474.
DR GeneID; 1025521; -.
DR KEGG; sfl:SF2340; -.
DR KEGG; sft:NCTC1_02574; -.
DR KEGG; sfx:S2474; -.
DR PATRIC; fig|198214.7.peg.2804; -.
DR HOGENOM; CLU_030273_0_1_6; -.
DR OMA; YEANRDG; -.
DR OrthoDB; 951991at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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:UniProtKB-UniRule.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 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; IPR010196; OSB_synthase_MenC1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..320
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_1000013813"
FT ACT_SITE 133
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
SQ SEQUENCE 320 AA; 35495 MW; FECA474802364B7A CRC64;
MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLREGERE GWGEISPLPG FSQENWEEAQ
SVLLAWVNNW LAGDCELPQM PSVAFGVSCA LAELTDTLPQ AANYRAAPLC NGDPDDLILK
LADMPGEKVA KVKVGLYEAV RDGMVVNLLL EAIPDLHLRL DANRAWTPLK GQQFAKYVNP
DYRHRIAFLE EPCKTRDDSR AFARETGIAI AWDESLREPD FAFVAEEGVR AVVIKPTLTG
SLEKVREQVQ AAHALGLTAV ISSSIESSLG LTQLARIAAW LTPDTIPGLD TLDLMQAQQV
RRWPGSPLPL VDADVQEQLL
