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Database: UniProt
Entry: A0A1J4U6F6_9BACT
LinkDB: A0A1J4U6F6_9BACT
Original site: A0A1J4U6F6_9BACT 
ID   A0A1J4U6F6_9BACT        Unreviewed;       369 AA.
AC   A0A1J4U6F6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000256|ARBA:ARBA00029491};
DE            EC=4.2.1.113 {ECO:0000256|ARBA:ARBA00029491};
GN   ORFNames=AUJ54_09275 {ECO:0000313|EMBL:OIO17839.1};
OS   Ignavibacteria bacterium CG1_02_37_35.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1805220 {ECO:0000313|EMBL:OIO17839.1, ECO:0000313|Proteomes:UP000182308};
RN   [1] {ECO:0000313|EMBL:OIO17839.1, ECO:0000313|Proteomes:UP000182308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_37_35 {ECO:0000313|EMBL:OIO17839.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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:OIO17839.1}.
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DR   EMBL; MNVA01000126; OIO17839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4U6F6; -.
DR   STRING; 1805220.AUJ54_09275; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000182308; Unassembled WGS sequence.
DR   GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
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   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; 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; 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.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          142..234
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   369 AA;  41202 MW;  0E7C658F8898341F CRC64;
     MLLDRITLYH IKMKLVSPFV TSLGTESNEE HIIIKVDGEG VTGWGECVAS ANPFYTYETV
     QTAWHNLSDF LIPGILRKNF NTLDEAIFSW QKVRGHNMAK AGLEAALWDF FAKTKNISLS
     KMLGGVRDKI DVGVSIGIQS SMNKLIKSVE GYLEEGYKRI KIKIQPGNDI QPIKASRIEF
     PNILLQVDAN SAYTLNDVKI FKAMDEFNLL LIEQPLGYED IYEHSKLQRE IKTPICLDES
     IRSLNDSRAA IELGSCKIIN IKPGRVGGFT EAKLIHDYCT SQNIPVWHGG MLESGIGRAG
     NVALASLPNF TLPGDISASK RYFKNDIVEP EFIINKDGTM NVPSKPGIGV EVNMKMLEKV
     TVRREEFSS
//
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