MENC_SALTY
ID MENC_SALTY Reviewed; 320 AA.
AC P58486;
DT 19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=STM2306;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL21207.1; -; Genomic_DNA.
DR RefSeq; NP_461248.1; NC_003197.2.
DR RefSeq; WP_001255561.1; NC_003197.2.
DR PDB; 3GC2; X-ray; 1.85 A; A=1-320.
DR PDBsum; 3GC2; -.
DR AlphaFoldDB; P58486; -.
DR SMR; P58486; -.
DR STRING; 99287.STM2306; -.
DR PaxDb; P58486; -.
DR EnsemblBacteria; AAL21207; AAL21207; STM2306.
DR GeneID; 1253828; -.
DR KEGG; stm:STM2306; -.
DR PATRIC; fig|99287.12.peg.2441; -.
DR HOGENOM; CLU_030273_0_1_6; -.
DR OMA; YEANRDG; -.
DR PhylomeDB; P58486; -.
DR BioCyc; SENT99287:STM2306-MON; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR EvolutionaryTrace; P58486; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..320
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000171275"
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"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 26..36
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:3GC2"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:3GC2"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:3GC2"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:3GC2"
SQ SEQUENCE 320 AA; 35360 MW; C88260F7A06C2FD8 CRC64;
MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLRDGERE GWGEISPLPG FSQETWEEAQ
TALLTWVNDW LQGSEGLPEM PSVAFGASCA LAELTGVLPE AADYRAAPLC TGDPDDLVLR
LADMPGEKIA KVKVGLYEAV RDGMVVNLLL EAIPDLHLRL DANRAWTPLK AQQFAKYVNP
DYRARIAFLE EPCKTRDDSR AFARETGIAI AWDESLREAD FTFEAEEGVR AVVIKPTLTG
SLDKVREQVA AAHALGLTAV ISSSIESSLG LTQLARIAAW LTPGTLPGLD TLHLMQAQQI
RPWPGSALPC LKREELERLL
