MENC_ECOLI
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 03-AUG-2022, entry version 178.
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; Proteobacteria; 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; P29208; -.
DR PRIDE; P29208; -.
DR EnsemblBacteria; AAC75321; AAC75321; b2261.
DR EnsemblBacteria; BAA16085; BAA16085; BAA16085.
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 PhylomeDB; P29208; -.
DR BioCyc; EcoCyc:O-SUCCINYLBENZOATE-COA-SYN-MON; -.
DR BioCyc; MetaCyc:O-SUCCINYLBENZOATE-COA-SYN-MON; -.
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 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_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
