MENC_SALPB
ID MENC_SALPB Reviewed; 320 AA.
AC A9N5A5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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}; OrderedLocusNames=SPAB_00675;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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: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; CP000886; ABX66101.1; -; Genomic_DNA.
DR RefSeq; WP_001255545.1; NC_010102.1.
DR AlphaFoldDB; A9N5A5; -.
DR SMR; A9N5A5; -.
DR KEGG; spq:SPAB_00675; -.
DR PATRIC; fig|1016998.12.peg.635; -.
DR HOGENOM; CLU_030273_0_1_6; -.
DR OMA; YEANRDG; -.
DR BioCyc; SENT1016998:SPAB_RS02805-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000008556; 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.
FT CHAIN 1..320
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_1000081205"
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; 35306 MW; 08C23B2B5B823107 CRC64;
MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLCDGERE GWGEISPLPG FSQETWEEAQ
TALLTWVNDW LQGNEGLPEM PSVAFGASCA LAELTGVLPE AADYRAAPLC TGDPDDLVLR
LADMPGEKIA KVKVGLYEAV RDGMVVNLLL EAIPDLHLRL DANRAWTPLK AQQFAKYVNP
DYRARIAFLE EPCKTRDDSR AFARETGIAI AWDESLREAD FTFEAEEGVK AVVIKPTLTG
SLDKVREQVA AAHALGLTVV ISSSIESSLG LTQLARIAAW LTPGTLPGLD TLHLMQAQQV
RPWPGSALPC LKRDELERLL
