ID E4QD31_CALH1 Unreviewed; 393 AA. AC E4QD31; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 54. DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:ADQ07525.1}; GN OrderedLocusNames=Calhy_1814 {ECO:0000313|EMBL:ADQ07525.1}; OS Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 / 108). OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales; OC Caldicellulosiruptoraceae; Caldicellulosiruptor. OX NCBI_TaxID=632292 {ECO:0000313|EMBL:ADQ07525.1, ECO:0000313|Proteomes:UP000006890}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=108; 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., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.; RT "Complete sequence of Caldicellulosiruptor hydrothermalis 108."; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADQ07525.1, ECO:0000313|Proteomes:UP000006890} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18901 / VKM B-2411 / 108 RC {ECO:0000313|Proteomes:UP000006890}; 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; CP002219; ADQ07525.1; -; Genomic_DNA. DR RefSeq; WP_013403680.1; NC_014652.1. DR AlphaFoldDB; E4QD31; -. DR STRING; 632292.Calhy_1814; -. DR KEGG; chd:Calhy_1814; -. DR eggNOG; COG0674; Bacteria. DR HOGENOM; CLU_002569_5_0_9; -. DR OrthoDB; 9794954at2; -. DR Proteomes; UP000006890; 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:ADQ07525.1}. 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; 43280 MW; A9887979D947D8AD CRC64; MAIRDRLSGN EAVAFAMKQI NPDVVAAFPI TPSTEVPQYF SQYVANGEVD TEFVAVESEH SAMSACIGAS AAGARTMTAT SSQGLALMWE MLYIAASMRL PIVMAVINRA LSGPINIHND HSDSMGARDS GWIQIYCENN QEAYDSLIQA IRIAEHKDVR LPVMVCYDGF ITSHAVENIE LLEDELVKKF VGEYNPEFYL LNEQNPISMG PLDLPPYYFE HKRQQAEAMK NAKKVVLEVA EEFAALTGRK YGLFEAYKLD DAEVAIVVMN STAGTAKAVV DEYRSKGYKV GLLKPRLFRP FPVDEIVGAL KHLKAVAIMD KSDGFNAAGG PLFTEITSAL YGRAEGIKAI NYIYGLGGRD VKTDDIAKVY DRLLDIVKTG NVGEVYNYIG VRE //