MENC_MYCS2
ID MENC_MYCS2 Reviewed; 321 AA.
AC A0QRG0; I7F7K1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=MSMEG_1103, MSMEI_1070;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK74303.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37550.1; -; Genomic_DNA.
DR RefSeq; WP_011727412.1; NZ_SIJM01000011.1.
DR RefSeq; YP_885498.1; NC_008596.1.
DR AlphaFoldDB; A0QRG0; -.
DR SMR; A0QRG0; -.
DR STRING; 246196.MSMEI_1070; -.
DR EnsemblBacteria; ABK74303; ABK74303; MSMEG_1103.
DR EnsemblBacteria; AFP37550; AFP37550; MSMEI_1070.
DR GeneID; 66732566; -.
DR KEGG; msg:MSMEI_1070; -.
DR KEGG; msm:MSMEG_1103; -.
DR PATRIC; fig|246196.19.peg.1091; -.
DR eggNOG; COG4948; Bacteria.
DR OMA; ANAAWDV; -.
DR OrthoDB; 951991at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 HAMAP; MF_00470; MenC_1; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR010196; OSB_synthase_MenC1.
DR InterPro; IPR041338; OSBS_N.
DR Pfam; PF18374; Enolase_like_N; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
PE 3: Inferred from homology;
KW Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..321
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_1000013805"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 138
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00470"
SQ SEQUENCE 321 AA; 33686 MW; 6AF928062C42A812 CRC64;
MTNGVPALDD ILERLHVVAL PMRVRFRGIT VRELALIDGP AGWGEFGAFV EYEPPEAAAW
LSSALEAAYR PAPAALRDRV PINATVPAVS AERVPEVLAR FPGARTAKVK VAEPGQSLAD
DVARVNAVRE SVPVVRVDAN GGWSVDDAVE AAAALTADGE LEYLEQPCAT VEELAALRAR
VDVPIAADES IRKAEDPLRV VRAHAADIAV LKVAPLGGVA RMLDIAAQID IPIVVSSALD
SSVGIGRGLL AAAALPELRH ACGLGTGGLF VDDVAEPRVP VDGCLAVEPA VPDPARLAAL
AAPEPRRQWW IDRVCACHAL I
