ID   MENC_ECOLI              Reviewed;         320 AA.
AC   P29208; P76476; P76931;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 184.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000303|PubMed:8335646};
DE            Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000305};
DE            Short=OSBS {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000303|PubMed:10194342};
DE            EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:10194342, ECO:0000269|PubMed:8335646};
DE   AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000305};
DE   AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000305};
GN   Name=menC {ECO:0000255|HAMAP-Rule:MF_00470};
GN   OrderedLocusNames=b2261, JW2256;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=K12;
RX   PubMed=8335646; DOI=10.1128/jb.175.15.4917-4921.1993;
RA   Sharma V., Meganathan R., Hudspeth M.E.S.;
RT   "Menaquinone (vitamin K2) biosynthesis: cloning, nucleotide sequence, and
RT   expression of the menC gene from Escherichia coli.";
RL   J. Bacteriol. 175:4917-4921(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10194342; DOI=10.1021/bi990140p;
RA   Palmer D.R., Garrett J.B., Sharma V., Meganathan R., Babbitt P.C.,
RA   Gerlt J.A.;
RT   "Unexpected divergence of enzyme function and sequence: 'N-acylamino acid
RT   racemase' is o-succinylbenzoate synthase.";
RL   Biochemistry 38:4252-4258(1999).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH 2-SUCCINYLBENZOIC
RP   ACID AND MAGNESIUM, COFACTOR, AND ACTIVE SITES.
RX   PubMed=10978150; DOI=10.1021/bi000855o;
RA   Thompson T.B., Garrett J.B., Taylor E.A., Meganathan R., Gerlt J.A.,
RA   Rayment I.;
RT   "Evolution of enzymatic activity in the enolase superfamily: structure of
RT   o-succinylbenzoate synthase from Escherichia coli in complex with Mg(2+)
RT   and o-Succinylbenzoate.";
RL   Biochemistry 39:10662-10676(2000).
CC   -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC       carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:10194342,
CC       PubMed:8335646). Does not show detectable N-acylamino acid racemase
CC       (NAAAR) activity with N-acetyl-S-methionine as substrate
CC       (PubMed:10194342). {ECO:0000269|PubMed:10194342,
CC       ECO:0000269|PubMed:8335646}.
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         ECO:0000269|PubMed:10194342, ECO:0000269|PubMed:8335646};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10978150};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Note=kcat is 19 sec(-1) with SHCHC as substrate.
CC         {ECO:0000269|PubMed:10194342};
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, ECO:0000269|PubMed:8335646}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:8335646}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. MenC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00470,
CC       ECO:0000305}.
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DR   EMBL; L07256; AAA71917.1; -; Unassigned_DNA.
DR   EMBL; U00096; AAC75321.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16085.2; -; Genomic_DNA.
DR   PIR; C64997; C64997.
DR   RefSeq; NP_416764.1; NC_000913.3.
DR   RefSeq; WP_001255628.1; NZ_LN832404.1.
DR   PDB; 1FHU; X-ray; 1.65 A; A=1-320.
DR   PDB; 1FHV; X-ray; 1.77 A; A=1-320.
DR   PDB; 1R6W; X-ray; 1.62 A; A=1-320.
DR   PDB; 2OFJ; X-ray; 2.30 A; A/B/C/D=1-320.
DR   PDBsum; 1FHU; -.
DR   PDBsum; 1FHV; -.
DR   PDBsum; 1R6W; -.
DR   PDBsum; 2OFJ; -.
DR   AlphaFoldDB; P29208; -.
DR   SMR; P29208; -.
DR   BioGRID; 4260503; 22.
DR   IntAct; P29208; 5.
DR   STRING; 511145.b2261; -.
DR   BindingDB; P29208; -.
DR   DrugBank; DB06864; 2-(3-CARBOXYPROPIONYL)-6-HYDROXY-CYCLOHEXA-2,4-DIENE CARBOXYLIC ACID.
DR   DrugBank; DB02251; O-Succinylbenzoate.
DR   jPOST; P29208; -.
DR   PaxDb; 511145-b2261; -.
DR   EnsemblBacteria; AAC75321; AAC75321; b2261.
DR   GeneID; 946734; -.
DR   KEGG; ecj:JW2256; -.
DR   KEGG; eco:b2261; -.
DR   PATRIC; fig|1411691.4.peg.4475; -.
DR   EchoBASE; EB1494; -.
DR   eggNOG; COG1441; Bacteria.
DR   HOGENOM; CLU_030273_0_1_6; -.
DR   InParanoid; P29208; -.
DR   OMA; YEANRDG; -.
DR   OrthoDB; 3725747at2; -.
DR   PhylomeDB; P29208; -.
DR   BioCyc; EcoCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER; -.
DR   BioCyc; MetaCyc:O-SUCCINYLBENZOATE-COA-SYN-MONOMER; -.
DR   BRENDA; 4.2.1.113; 2026.
DR   SABIO-RK; P29208; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   EvolutionaryTrace; P29208; -.
DR   PRO; PR:P29208; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016836; F:hydro-lyase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
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; IPR013342; Mandelate_racemase_C.
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; SFLDG00180; muconate_cycloisomerase; 1.
DR   SFLD; SFLDF00009; o-succinylbenzoate_synthase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 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_0000171270"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT                   ECO:0000269|PubMed:10978150"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT                   ECO:0000269|PubMed:10978150"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT                   ECO:0000269|PubMed:10978150"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT                   ECO:0000269|PubMed:10978150"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00470,
FT                   ECO:0000269|PubMed:10978150"
FT   CONFLICT        176..177
FT                   /note="Missing (in Ref. 1; AAA71917)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2..13
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          26..36
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          39..45
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:1FHU"
FT   HELIX           56..70
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           81..94
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:1FHU"
FT   HELIX           114..122
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          126..133
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           139..152
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          156..161
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           168..176
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           183..185
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           196..206
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           214..217
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           236..239
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          258..262
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           268..281
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           292..294
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   HELIX           313..315
FT                   /evidence="ECO:0007829|PDB:1R6W"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:1R6W"
SQ   SEQUENCE   320 AA;  35477 MW;  E20245EC13D06839 CRC64;
     MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLREGERE GWGEISPLPG FSQETWEEAQ
     SVLLAWVNNW LAGDCELPQM PSVAFGVSCA LAELTDTLPQ AANYRAAPLC NGDPDDLILK
     LADMPGEKVA KVKVGLYEAV RDGMVVNLLL EAIPDLHLRL DANRAWTPLK GQQFAKYVNP
     DYRDRIAFLE EPCKTRDDSR AFARETGIAI AWDESLREPD FAFVAEEGVR AVVIKPTLTG
     SLEKVREQVQ AAHALGLTAV ISSSIESSLG LTQLARIAAW LTPDTIPGLD TLDLMQAQQV
     RRWPGSTLPV VEVDALERLL
//