ID D7GCL8_PROFC Unreviewed; 332 AA.
AC D7GCL8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:CBL56279.1};
GN OrderedLocusNames=PFREUD_07480 {ECO:0000313|EMBL:CBL56279.1};
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56279.1, ECO:0000313|Proteomes:UP000000936};
RN [1] {ECO:0000313|EMBL:CBL56279.1, ECO:0000313|Proteomes:UP000000936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC {ECO:0000313|Proteomes:UP000000936};
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(2010).
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; FN806773; CBL56279.1; -; Genomic_DNA.
DR RefSeq; WP_013160664.1; NC_014215.1.
DR AlphaFoldDB; D7GCL8; -.
DR STRING; 754252.PFREUD_07480; -.
DR GeneID; 61222559; -.
DR KEGG; pfr:PFREUD_07480; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_057696_0_0_11; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000000936; Chromosome.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000936}.
FT DOMAIN 99..196
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ SEQUENCE 332 AA; 35170 MW; 0E88D83232147CD0 CRC64;
MKSAALTHVQ VPEALRRRGI DEVLVFQAGL RHRFRRIEVR DGLLLHGEQG WGECSPFWDY
GATESASWLH AGLEAATRPL PAPVRDLVEV NVTIPVVSPT QARRLIAASG GCMTAKVKVA
DPGSDLRQDC ARVAAARAEL GPEGRIRVDA NAAWSVDEAV AAVIELDAAA EGLEYVEQPC
PSVEELARVR RRITVPVAAD ESVRRADDPV AVARAGAADI VIVKAQPLGG VARALDVVDR
AGLDAVVSSA LDTSVGLGIG TALAASLPRL GHACGLATIE LFTGDVTTSP LLPEGGALVP
RRVEADQPVH QDVPRALVDR WVERLTAICH EL
//
