ID K0NKY2_DESTT Unreviewed; 381 AA. AC K0NKY2; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 40. DE SubName: Full=PorA: pyruvate synthase, alpha subunit {ECO:0000313|EMBL:CCK82241.1}; DE EC=1.2.7.1 {ECO:0000313|EMBL:CCK82241.1}; GN Name=porA {ECO:0000313|EMBL:CCK82241.1}; GN OrderedLocusNames=TOL2_C40850 {ECO:0000313|EMBL:CCK82241.1}; OS Desulfobacula toluolica (strain DSM 7467 / Tol2). OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulfobacula. OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK82241.1, ECO:0000313|Proteomes:UP000007347}; RN [1] {ECO:0000313|EMBL:CCK82241.1, 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). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FO203503; CCK82241.1; -; Genomic_DNA. DR RefSeq; WP_014959421.1; NC_018645.1. DR AlphaFoldDB; K0NKY2; -. DR STRING; 651182.TOL2_C40850; -. DR KEGG; dto:TOL2_C40850; -. DR PATRIC; fig|651182.5.peg.4810; -. DR HOGENOM; CLU_002569_5_0_7; -. DR OrthoDB; 9794954at2; -. DR Proteomes; UP000007347; Chromosome. DR GO; GO:0019164; F:pyruvate 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; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1. DR PANTHER; PTHR32154:SF0; 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 Oxidoreductase {ECO:0000313|EMBL:CCK82241.1}; KW Pyruvate {ECO:0000313|EMBL:CCK82241.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000007347}. FT DOMAIN 19..233 FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase FT pyrimidine binding" FT /evidence="ECO:0000259|Pfam:PF01855" FT DOMAIN 257..360 FT /note="Pyruvate:ferredoxin oxidoreductase core" FT /evidence="ECO:0000259|Pfam:PF17147" SQ SEQUENCE 381 AA; 42442 MW; 49CCFB67BC7B0551 CRC64; MKRVLTGNNS ACWGIRLSRV KLIAAYPIPT QVHIMEELSI MCKDGSLDAR FLQLESESSA LAAVIASQTT GIRSFIACSL NSLSHMHDLL YRAAGARLPI VMLTVKKSLE SGGHIGSDQA DALIQRDTGW IQMYVENNQE VLDSVIQAYR IAEKVHLPVM ICYDDLFSGH VCEPVDIPGQ DEADTFLPSY EPEFFLDPKN PKSFYSQLLP DNYMDMLYQL QTAHEKALDI IDETGKSFKK ILGRSCGVVE NIECKDAQIV LVVHGAMTCP ARHILKQMRK KGQKMGVLKI RIFRPFPVTA VQTALKGCKK VIVIDKNYSL GKGGIFADEL KSAISDVPDA PLVYSYIAGL REKNIALEDI REMINETISR DTPPRHSVWK G //