ID E4SFV2_CALK2 Unreviewed; 393 AA. AC E4SFV2; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 48. DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:ADQ46627.1}; GN OrderedLocusNames=Calkro_1778 {ECO:0000313|EMBL:ADQ46627.1}; OS Caldicellulosiruptor kronotskyensis (strain DSM 18902 / VKM B-2412 / 2002). OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales; OC Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=632348 {ECO:0000313|EMBL:ADQ46627.1, ECO:0000313|Proteomes:UP000006835}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=2002; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., RA Blumer-Schuette S.E., Kelly R.M., Woyke T.; RT "Complete sequence of Caldicellulosiruptor kronotskyensis 2002."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADQ46627.1, ECO:0000313|Proteomes:UP000006835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18902 / VKM B-2412 / 2002 RC {ECO:0000313|Proteomes:UP000006835}; RX PubMed=21216991; DOI=10.1128/JB.01515-10; RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A., RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T., RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C., RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.; RT "Complete genome sequences for the anaerobic, extremely thermophilic plant RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis, RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis, RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus."; RL J. Bacteriol. 193:1483-1484(2011). 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; CP002330; ADQ46627.1; -; Genomic_DNA. DR RefSeq; WP_013430715.1; NC_014720.1. DR AlphaFoldDB; E4SFV2; -. DR KEGG; ckn:Calkro_1778; -. DR PATRIC; fig|632348.3.peg.1875; -. DR HOGENOM; CLU_002569_5_0_9; -. DR OrthoDB; 9794954at2; -. DR Proteomes; UP000006835; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 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 Pyruvate {ECO:0000313|EMBL:ADQ46627.1}. FT DOMAIN 16..240 FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase FT pyrimidine binding" FT /evidence="ECO:0000259|Pfam:PF01855" FT DOMAIN 262..366 FT /note="Pyruvate:ferredoxin oxidoreductase core" FT /evidence="ECO:0000259|Pfam:PF17147" SQ SEQUENCE 393 AA; 43333 MW; D4E7D2E7BC01C406 CRC64; MAIRDRLSGN EAIALAMKQI NPDVVAAFPI TPSTEVPQYF SQYVANGEVD TEFVAVESEH SAMSACIGAS AAGARTMTAT SSQGLALMWE MLYIAASMRL PIVMAVINRA LSGPINIHND HSDSMGARDS GWIQIYCENN QEAYDSLIQA IRIAEHKDVR LPVMVCYDGF ITSHAVENIE LLEDELVKKF VGEYNPEFYL LNEQNPISMG PLDLPPYYFE HKRQQAEAMR NAKKVVLEVA EEFAALTGRK YGLFESYKLD DAEVAIVVMN STAGTAKAVV DEYRSKGYKV GLLKPRLFRP FPVDEIVGVL KHLKAIAIMD KSDGFNAAGG PLFTEITSAL YGRADGIKAI NYIYGLGGRD VKTDDIAKVY DRLLDIVKTG NVGEVYNYIG VRE //