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Database: UniProt
Entry: K0NEW0_DESTT
LinkDB: K0NEW0_DESTT
Original site: K0NEW0_DESTT 
ID   K0NEW0_DESTT            Unreviewed;       375 AA.
AC   K0NEW0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=KorA2: 2-oxoglutarate synthase, subunit A {ECO:0000313|EMBL:CCK79475.1};
DE            EC=1.2.7.3 {ECO:0000313|EMBL:CCK79475.1};
GN   Name=korA2 {ECO:0000313|EMBL:CCK79475.1};
GN   OrderedLocusNames=TOL2_C13120 {ECO:0000313|EMBL:CCK79475.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79475.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK79475.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
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DR   EMBL; FO203503; CCK79475.1; -; Genomic_DNA.
DR   RefSeq; WP_014956822.1; NC_018645.1.
DR   AlphaFoldDB; K0NEW0; -.
DR   STRING; 651182.TOL2_C13120; -.
DR   KEGG; dto:TOL2_C13120; -.
DR   PATRIC; fig|651182.5.peg.1580; -.
DR   HOGENOM; CLU_017038_0_1_7; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000007347; Chromosome.
DR   GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR32154:SF14; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORA; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000313|EMBL:CCK79475.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT   DOMAIN          15..238
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          272..364
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   COILED          246..273
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   375 AA;  40681 MW;  42AA021B7A2B330A CRC64;
     MAISFMDGNE ALARGAIAAG CNFFAGYPIT PATTILNNML KMLPPKGGIC VQAEDEIASM
     GYCIGAAMAG KKALTATSGP GISLYSEQIS FAIGSEIPLV IADVQRLGPS TGSATRGADG
     DIQFLRWGNS GGVPVIVLVP ADAKDCYVLA FHAFNYAEEF RCPVFIASNK EIGMTKQSID
     LESITLPKIV ARNLFSESTY LPFEAKPDAA PPFLPIGGKT IVRQTSSTHG PDGYLTIDPD
     VIAQNQARLR KKIHKARNRI TLFEENIKET SDTLVISYGI TSRSVKNAAK RLEKKGKAVS
     TLNLKSLWPV PEDLLIKKAK PFTRIAVIEM NLGQYVKEIQ RVLCDKKIGF YGQMNGQLIT
     PSKIMEVIEN ESLFK
//
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