ID A9BH89_PETMO Unreviewed; 389 AA. AC A9BH89; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 82. DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:ABX31319.1}; GN OrderedLocusNames=Pmob_0585 {ECO:0000313|EMBL:ABX31319.1}; OS Petrotoga mobilis (strain DSM 10674 / SJ95). OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae; OC Petrotoga. OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX31319.1, ECO:0000313|Proteomes:UP000000789}; RN [1] {ECO:0000313|EMBL:ABX31319.1, ECO:0000313|Proteomes:UP000000789} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Noll K., Richardson P.; RT "Complete sequence of Petroga mobilis SJ95."; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000879; ABX31319.1; -; Genomic_DNA. DR RefSeq; WP_012208423.1; NC_010003.1. DR AlphaFoldDB; A9BH89; -. DR STRING; 403833.Pmob_0585; -. DR KEGG; pmo:Pmob_0585; -. DR eggNOG; COG0674; Bacteria. DR HOGENOM; CLU_002569_5_0_0; -. DR OrthoDB; 9794954at2; -. DR Proteomes; UP000000789; 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:ABX31319.1}. FT DOMAIN 15..235 FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase FT pyrimidine binding" FT /evidence="ECO:0000259|Pfam:PF01855" FT DOMAIN 262..364 FT /note="Pyruvate:ferredoxin oxidoreductase core" FT /evidence="ECO:0000259|Pfam:PF17147" SQ SEQUENCE 389 AA; 43314 MW; 9082A41C5BCC617E CRC64; MPVKLTVTGA AAVAHAMRQI NPDVVAAYPI TPQTPIVEYY AGFVSDGIVD TILVPVESEH SAMSAVIGSA ASGARTMTAT AANGLALMLE IVYIAASYRL PIIMPVVNRA LSGPINIHCD HSDAMMARDS GWIQFFTENH QEAYDFTIMA TKLAEKENVL LPAMVNLDGF ITSHGVESFE MLDDEVVREF VGSWNPKYSL LDTKNPVSFG PLDLFDYYFE HHRQQEEAMT NAYKELPRVF EEFEKISGRR YDFLDLYKVN DADYIMVVMN STASTAKYVV DQLREEGHKV GLVKPQVFTP FPKKEFQQAL NGRKGVVVLD RAMSFGKEAP LYSLVKSSLY EVASRPSLGS YIYGLGGRDT TPEMIREAFE DALQGNLIAD EQRYLGLRE //