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Database: UniProt
Entry: G7HZW2_9CORY
LinkDB: G7HZW2_9CORY
Original site: G7HZW2_9CORY 
ID   G7HZW2_9CORY            Unreviewed;       341 AA.
AC   G7HZW2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE            Short=OSB synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE            Short=OSBS {ECO:0000256|HAMAP-Rule:MF_00470};
DE            EC=4.2.1.113 {ECO:0000256|HAMAP-Rule:MF_00470};
DE   AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00470};
DE   AltName: Full=o-succinylbenzoic acid synthase {ECO:0000256|HAMAP-Rule:MF_00470};
GN   Name=menC {ECO:0000256|HAMAP-Rule:MF_00470,
GN   ECO:0000313|EMBL:CCE55727.1};
GN   ORFNames=CCAS_11215 {ECO:0000313|EMBL:CCE55727.1};
OS   Corynebacterium casei UCMA 3821.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1110505 {ECO:0000313|EMBL:CCE55727.1, ECO:0000313|Proteomes:UP000004840};
RN   [1] {ECO:0000313|EMBL:CCE55727.1, ECO:0000313|Proteomes:UP000004840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCMA 3821 {ECO:0000313|EMBL:CCE55727.1,
RC   ECO:0000313|Proteomes:UP000004840};
RX   PubMed=22247534; DOI=10.1128/JB.06496-11;
RA   Monnet C., Loux V., Bento P., Gibrat J.F., Straub C., Bonnarme P.,
RA   Landaud S., Irlinger F.;
RT   "Genome Sequence of Corynebacterium casei UCMA 3821, Isolated from a Smear-
RT   Ripened Cheese.";
RL   J. Bacteriol. 194:738-739(2012).
CC   -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC       carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00470};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00470}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00470}.
CC   -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC       enzyme family. MenC type 1 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00470}.
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DR   EMBL; CAFW01000086; CCE55727.1; -; Genomic_DNA.
DR   RefSeq; WP_006823175.1; NZ_CAFW01000086.1.
DR   AlphaFoldDB; G7HZW2; -.
DR   GeneID; 82876693; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000004840; Unassembled WGS sequence.
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   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; IPR010196; OSB_synthase_MenC1.
DR   InterPro; IPR041338; OSBS_N.
DR   PANTHER; PTHR48073:SF2; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR   PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR   Pfam; PF18374; Enolase_like_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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00470};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00470};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00470};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00470}.
FT   DOMAIN          86..184
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        105
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   ACT_SITE        217
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ   SEQUENCE   341 AA;  37026 MW;  0FF426DEE9A86F64 CRC64;
     MQIDDILDRA HVVALPLAVK FRGITTREAL LIDGPAGWGE FSPFVEYGPQ ESASWLAAGL
     EAAYEGFPEL VRDRVEVNGT IPAVAAEQVP ELMNRYPGVR TWKVKVAEPG QSLHDDIARV
     NAVREYASEH NPSLSPIIRV DANGGWSVEE AIAAAKEMMP LDYMEQPCRT AEELAEVRSQ
     LMRNGLFVRV AADESIRKAN DPYRVAELQA ADVAIVKPAP LGGVRKTLEI ARNLRARHMD
     VTVASALDTA VGISMGLATV AALPKIYDDE DIDVIPSAAG LATGSLFLED VAAPRQLVGG
     ALPAAPIAAE LDRLEALVAP AERRDWWFNR VRECYSVLNS K
//
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