ID A0A1F1IHQ6_9MICC Unreviewed; 357 AA.
AC A0A1F1IHQ6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=HMPREF2863_04755 {ECO:0000313|EMBL:OFR91410.1};
OS Micrococcus sp. HMSC067E09.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=1739367 {ECO:0000313|EMBL:OFR91410.1, ECO:0000313|Proteomes:UP000177882};
RN [1] {ECO:0000313|EMBL:OFR91410.1, ECO:0000313|Proteomes:UP000177882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC067E09 {ECO:0000313|EMBL:OFR91410.1,
RC ECO:0000313|Proteomes:UP000177882};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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:OFR91410.1}.
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DR EMBL; LTYF01000002; OFR91410.1; -; Genomic_DNA.
DR RefSeq; WP_070638397.1; NZ_KV809432.1.
DR AlphaFoldDB; A0A1F1IHQ6; -.
DR STRING; 1739367.HMPREF2863_04755; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000177882; 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:UP000177882}.
FT DOMAIN 101..207
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ SEQUENCE 357 AA; 37443 MW; B2ADC3ED6F01C2A7 CRC64;
MSADTVLPPL PGAPGGPSLP SVEELLEHAV AVSLPMTVRF RGTTRREALL LHGPAGWAEF
SPFPEYGDEE SSRWMAAAVE AGWQGWPEPV RDAVPVNATV PAVAAEDVER VLATYGEGIT
AVKVKVAEHG PDGRLVAGSR EEDLARVRRV RELLPQASLR VDANMGWTHE QAVDVLTELE
DVGLEYAEQP VPGIEPLAAV RRELRERGVP TRIAADEAVR KEADPLAVAQ ADAADLIVVK
VQPLGGVRRA AAIVEAAGLD AVVSSALDTS VGLAGSAALA AHLPRLPFAC GLGTGALFSR
DVCDPAWTPS GGMLPVPGVS APEPDPALLE AVRADAASHD RWARRVHGAH AVLAAQH
//
