ID A0A364K493_9BACL Unreviewed; 369 AA.
AC A0A364K493;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:RAL24208.1};
GN ORFNames=DL897_11045 {ECO:0000313|EMBL:RAL24208.1};
OS Thermoflavimicrobium daqui.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoflavimicrobium.
OX NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL24208.1, ECO:0000313|Proteomes:UP000251213};
RN [1] {ECO:0000313|EMBL:RAL24208.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL24208.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Wang X., Zhou H.;
RT "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT Moutai-flavour Daqu.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAL24208.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL24208.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Zhirakovskaya E.;
RL Submitted (JUN-2018) 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:RAL24208.1}.
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DR EMBL; QJKK01000005; RAL24208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364K493; -.
DR OrthoDB; 9774531at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000251213; 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:UP000251213}.
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 369 AA; 42048 MW; 9E19F3E0E6C77BCC CRC64;
MNIHSITLRK MNMPLKAPFT TSFGTFKQKD FILVEIRDQE GLSGWAESVA FTSPWYNEET
IETNWHMIKD FLIPLLLEKD IQHPHEVSQR FAHIRRNYMA KSALEGAIWD LFAKRQQLPL
AKALGGKKKQ IEVGVSIGIQ NSVQELLTII ERHVSAGYHR IKVKIKPGWD IEIIREIRNH
FPNILLMADA NSAYRLTDTQ RLKELDEFNL MMIEQPLAPD DIIDHAYLQR QLTTPICLDE
SIHSVEDARK ALALGSCQII NIKIGRVGGL TEAMKIHDLC ETQKIPVWCG GMLESGIGRA
HNIALTTLSN FTLPGDTAAS SNYWYQDLIE PEVTVNRGII HVPEEWGIGY EPNRLAIDQF
TQYSETLRP
//
