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Database: UniProt
Entry: S3XAQ2_9ACTN
LinkDB: S3XAQ2_9ACTN
Original site: S3XAQ2_9ACTN 
ID   S3XAQ2_9ACTN            Unreviewed;       329 AA.
AC   S3XAQ2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=HMPREF1531_00264 {ECO:0000313|EMBL:EPH07211.1};
OS   Propionibacterium sp. oral taxon 192 str. F0372.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH07211.1, ECO:0000313|Proteomes:UP000014567};
RN   [1] {ECO:0000313|EMBL:EPH07211.1, ECO:0000313|Proteomes:UP000014567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0372 {ECO:0000313|EMBL:EPH07211.1,
RC   ECO:0000313|Proteomes:UP000014567};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA   Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL   Submitted (MAY-2013) 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:EPH07211.1}.
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DR   EMBL; ATFL01000001; EPH07211.1; -; Genomic_DNA.
DR   RefSeq; WP_016668079.1; NZ_KE340297.1.
DR   AlphaFoldDB; S3XAQ2; -.
DR   STRING; 1203605.HMPREF1531_00264; -.
DR   PATRIC; fig|1203605.3.peg.266; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_057696_0_0_11; -.
DR   OrthoDB; 3725747at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000014567; 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:0009063; P:amino acid catabolic process; IEA:InterPro.
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; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
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.
DR   PROSITE; PS00909; MR_MLE_2; 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:UP000014567}.
FT   DOMAIN          81..175
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         156
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
FT   BINDING         184
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00470"
SQ   SEQUENCE   329 AA;  35919 MW;  8B2E6F44C9B961EB CRC64;
     MTEPFDEIIV YAIPMRSRFR GIDVRHGMLL RRGDRWSEWS PFPEYGDREA ATWLCAALLT
     DDPVIVRERV PVNVTIPVVS PSRAAELVSA AGCTTAKVKV AGAGSSQADD LARLDAVRNA
     LGASGRIRID ANGAWTPIRA AEAITSMARI GLEYVEQPCA SVDELAELRE MLAHKGVGVP
     VAADESVRRA ADPHLVVARN AADLLVIKNQ PLGGWRRCLE LADFGLPMVV SSALETSIGL
     YDSLRLAAAL PVLDHACGIN TARLFTDDVV TSSLIARDGH LEIGPRPVVD HQRAATLKAD
     RTTTRWWRDR LERCLDLARQ FNSAEQEES
//
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