ID A0A0A6VH60_9BACI Unreviewed; 373 AA.
AC A0A0A6VH60;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000256|ARBA:ARBA00029491, ECO:0000256|HAMAP-Rule:MF_01933};
DE Short=OSB synthase {ECO:0000256|HAMAP-Rule:MF_01933};
DE Short=OSBS {ECO:0000256|HAMAP-Rule:MF_01933};
DE EC=4.2.1.113 {ECO:0000256|ARBA:ARBA00029491, ECO:0000256|HAMAP-Rule:MF_01933};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000256|HAMAP-Rule:MF_01933};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000256|HAMAP-Rule:MF_01933};
GN Name=menC {ECO:0000256|HAMAP-Rule:MF_01933,
GN ECO:0000313|EMBL:NEY21029.1};
GN ORFNames=G4D61_13815 {ECO:0000313|EMBL:NEY21029.1}, NG54_06230
GN {ECO:0000313|EMBL:KHD85964.1};
OS Heyndrickxia ginsengihumi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=363870 {ECO:0000313|EMBL:KHD85964.1, ECO:0000313|Proteomes:UP000030588};
RN [1] {ECO:0000313|EMBL:KHD85964.1, ECO:0000313|Proteomes:UP000030588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2.11 {ECO:0000313|EMBL:KHD85964.1,
RC ECO:0000313|Proteomes:UP000030588};
RA Toymentseva A., Boulygina E.A., Kazakov S.V., Kayumov I., Suleimanova A.D.,
RA Mardanova A.M., Maria S.N., Sergey M.Y., Sharipova M.R.;
RT "Draft genome of phytase producing Bacillus ginsengihumi strain M2.11.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NEY21029.1, ECO:0000313|Proteomes:UP000476934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 114 {ECO:0000313|EMBL:NEY21029.1,
RC ECO:0000313|Proteomes:UP000476934};
RA Feng H.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:NEY21029.1, ECO:0000313|Proteomes:UP000476934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 114 {ECO:0000313|EMBL:NEY21029.1,
RC ECO:0000313|Proteomes:UP000476934};
RA Xie J.;
RT "Bacillus aquiflavi sp. nov., isolated from yellow water of strong flavor
RT Chinese baijiu in Yibin region of China.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000256|HAMAP-
CC Rule:MF_01933}.
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_01933};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968,
CC ECO:0000256|HAMAP-Rule:MF_01933};
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_01933}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01933}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01933}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHD85964.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRUN01000013; KHD85964.1; -; Genomic_DNA.
DR EMBL; JAAIWK010000024; NEY21029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6VH60; -.
DR STRING; 363870.NG54_06230; -.
DR OrthoDB; 9774531at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000030588; Unassembled WGS sequence.
DR Proteomes; UP000476934; 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; cd03317; NAAAR; 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_01933; MenC_2; 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; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR047585; MenC.
DR InterPro; IPR010197; OSBS/NAAAR.
DR NCBIfam; TIGR01928; menC_lowGC_arch; 1.
DR PANTHER; PTHR48073:SF5; O-SUCCINYLBENZOATE SYNTHASE; 1.
DR PANTHER; PTHR48073; O-SUCCINYLBENZOATE SYNTHASE-RELATED; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 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 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_01933, ECO:0000313|EMBL:NEY21029.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01933};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01933};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01933}; Reference proteome {ECO:0000313|Proteomes:UP000030588}.
FT DOMAIN 143..235
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 164
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
SQ SEQUENCE 373 AA; 41822 MW; 3CEB5FDEABCB243E CRC64;
MMKIQHVHLS IIKMPLKSPF ANALETVTER ESIILEVIDH DGVAGYGEVV AFSTPWYTEE
TVKTCYHLLK DVLIPIVLDR AIEHPKEISE RFQAVRGNPM AKAGIETAIW DLYAKRKNLP
LWKLIGGTRE SVLSGVVVGT HDSKSALNQI EQFMLEGYDR VKVKIKPGHD YDFLQLIRTH
YPYLSLMADA NSSYTLNDLP LLKSLDRFNL LMIEQPLAVD DIVEHAALQK QMQTPICLDE
SIVTYHDAES AIRLGSMGVL NIKIGRVGGL WNAIQLHNLC LKHSIPVWCG GMIEFGISRA
FNIALATLEG FTIPGDISSS NRFWEKDIIT PEVHVRKGKI QAPMQAGIGF NINKKQLIAA
TIYSEKIVKR GLQ
//
