ID A0A1I0ZWT4_9BACI Unreviewed; 371 AA.
AC A0A1I0ZWT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=SAMN04488072_11361 {ECO:0000313|EMBL:SFB28900.1};
OS Lentibacillus halodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=237679 {ECO:0000313|EMBL:SFB28900.1, ECO:0000313|Proteomes:UP000198642};
RN [1] {ECO:0000313|EMBL:SFB28900.1, ECO:0000313|Proteomes:UP000198642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3702 {ECO:0000313|EMBL:SFB28900.1,
RC ECO:0000313|Proteomes:UP000198642};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOJW01000013; SFB28900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0ZWT4; -.
DR STRING; 237679.SAMN04488072_11361; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000198642; 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; SFLDS00001; Enolase; 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};
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:UP000198642}.
FT DOMAIN 145..237
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01933"
SQ SEQUENCE 371 AA; 41878 MW; DB84B84577529214 CRC64;
MTIPVKQIKL RRIKMMLNDP FTTSFGTMQE KEFFITEVLD NDGNHGFGES VAFTSPWYSE
ETVETNHHIM KDFLIQRLRK NILHHPDDVL EVFKPIKRNN MAKSALEGAI WDLYAKQNQI
PLAEALGGTK KEIDVGISIG IQPSVNDLLQ TIDHYVKEGY KRIKIKIKPG WDYDVLKEVR
KHFPETPIMA DANSAYTLKD IDQLKKLDEL DLMMIEQPLA HNDIVDHAKL QATLGTPICL
DESIHSLEDV RKAIELKSCS IINIKIGRVG GLSEAKRIQD LCQKHDIDVW CGGMLEAGVG
RAHNIALTTL PQFVLPGDTA GSSRYWKKDI IKPEVTVHDG MIAVPDKPGI GYEIDDEALD
AFTVKEEIFN L
//
