ID A0A1G6GG47_9ACTN Unreviewed; 317 AA.
AC A0A1G6GG47;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ORFNames=GA0111570_10342 {ECO:0000313|EMBL:SDB80725.1};
OS Raineyella antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Raineyella.
OX NCBI_TaxID=1577474 {ECO:0000313|EMBL:SDB80725.1, ECO:0000313|Proteomes:UP000199086};
RN [1] {ECO:0000313|EMBL:SDB80725.1, ECO:0000313|Proteomes:UP000199086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LZ-22 {ECO:0000313|EMBL:SDB80725.1,
RC ECO:0000313|Proteomes:UP000199086};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-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_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; FMYF01000003; SDB80725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6GG47; -.
DR STRING; 1577474.GA0111570_10342; -.
DR OrthoDB; 3725747at2; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000199086; 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 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 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; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000199086}.
FT DOMAIN 79..173
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ SEQUENCE 317 AA; 33903 MW; 12681DDD40E0B1E6 CRC64;
MDTYVYAIPL RTRFRGIDVR EGLLWEGPAG WAEWSPFLDY SGAELVPWLR AAREAAERPW
PAPVRDRVPV NVTVPVVGPD QAHAIVTGSG CRTAKVKVAD PRTVLAEDIA RLEAVRDALG
PAGRLRIDAN GAWDVDTARR NLAELARFDL EYAEQPCPDV EDLAALRRHL AHDGIDVPIA
ADESIRRSGD PERVVALEAA DVAVLKVQPL GGVAACLELA ERLGLPVVVS SALETSVGLA
AGLALAAALP ELPYACGLNT SRLLVDDVVD EPLAAVDGWM EVRRPVPTPT RLAALAADPA
TAGKWARRRE ATGRLAG
//
