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Database: UniProt
Entry: A0A124IVT8_9BACL
LinkDB: A0A124IVT8_9BACL
Original site: A0A124IVT8_9BACL 
ID   A0A124IVT8_9BACL        Unreviewed;       375 AA.
AC   A0A124IVT8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=o-succinylbenzoate synthase {ECO:0000256|ARBA:ARBA00029491};
DE            EC=4.2.1.113 {ECO:0000256|ARBA:ARBA00029491};
GN   ORFNames=ATW55_04300 {ECO:0000313|EMBL:KUO95311.1};
OS   Ferroacidibacillus organovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Ferroacidibacillus.
OX   NCBI_TaxID=1765683 {ECO:0000313|EMBL:KUO95311.1, ECO:0000313|Proteomes:UP000053557};
RN   [1] {ECO:0000313|EMBL:KUO95311.1, ECO:0000313|Proteomes:UP000053557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ITV001 {ECO:0000313|EMBL:KUO95311.1,
RC   ECO:0000313|Proteomes:UP000053557};
RA   Dall'Agnol H., Nancucheo I., Johnson B., Oliveira R., Leite L., Pylro V.,
RA   Nunes G.L., Tzotzos G., Fernandes G.R., Dutra J., Orellana S.C.,
RA   Oliveira G.;
RT   "Draft genome sequence of Acidibacillus ferrooxidans ITV001, isolated from
RT   a chalcopyrite acid mine drainage site in Brazil.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO95311.1}.
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DR   EMBL; LPVJ01000053; KUO95311.1; -; Genomic_DNA.
DR   RefSeq; WP_067717660.1; NZ_LPVJ01000053.1.
DR   AlphaFoldDB; A0A124IVT8; -.
DR   OrthoDB; 9774531at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00165.
DR   Proteomes; UP000053557; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          146..238
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   375 AA;  41419 MW;  DC83E024E5B70730 CRC64;
     MQIASVSLQR VRLPLKEPFV TSFGIEDARE GIIVTVRTVR GGIGYGECVA SMEPLYSEET
     NATAWHMLRD FFIPALQSHA YNSVQDLRDI RLKLAHFKRN KMAKAAIEMA IWDAYANESA
     TPIATLLGGT RTEIPVGISI GIQPNLDTLI ERVGYYVSQG FARVKLKVRP GFDFEPLRVI
     RESFPDMPLM ADANSAYCLK DVRHLKKWDA LNLMMIEQPL AHDDIMDHAK LQAELATPIC
     LDESINSAED LRKALEIGAC RIVNLKVGRV GGFGEALAIH DRCREAGVDM WCGGMLESGI
     GRLHNVALTA LPGFTLPGDT APSARYFEED LIQPAVTFLR PGVLAVEPLS GVASRVDQER
     LEKYTIQVAE VVSAR
//
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