ID   A0A1G7WXK2_9RHOO        Unreviewed;      1662 AA.
AC   A0A1G7WXK2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Pyruvate-ferredoxin/flavodoxin oxidoreductase {ECO:0000313|EMBL:SDG76626.1};
GN   ORFNames=SAMN05660652_00666 {ECO:0000313|EMBL:SDG76626.1};
OS   Propionivibrio dicarboxylicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Propionivibrio.
OX   NCBI_TaxID=83767 {ECO:0000313|EMBL:SDG76626.1, ECO:0000313|Proteomes:UP000198607};
RN   [1] {ECO:0000313|EMBL:SDG76626.1, ECO:0000313|Proteomes:UP000198607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5885 {ECO:0000313|EMBL:SDG76626.1,
RC   ECO:0000313|Proteomes:UP000198607};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNCY01000001; SDG76626.1; -; Genomic_DNA.
DR   STRING; 83767.SAMN05660652_00666; -.
DR   OrthoDB; 9794954at2; -.
DR   Proteomes; UP000198607; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd14688; bZIP_YAP; 1.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
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; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:SDG76626.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198607};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          841..871
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          972..1001
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   COILED          1077..1104
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1662 AA;  178954 MW;  65406D2F4CD11DED CRC64;
     MKAKKAKYPG IPTVINGNGA VAHVMGQVCG GVIGYPITPS TEISEIYEAF RAEGGVNVWG
     KHPFFFEPEG EHSAQSGALG AQLTGGQYIS NASSSQGILY ALESHYVTVG KKVGGFVLQV
     AARVVSKHSL NVMAGHDDVY ALLSSGYTIL FGSNPQEAAD LAAISYRSSA LSLIPVANAM
     DGFATSHMMS ESYLPEPELL KEYLGDPEGR IKAPTVAQEV LFGAKGRVFQ LNQYLSRHEA
     DITADNLAAL KKYLDSNAAK VEKDNAGELV AKTLGWLPEE LHGQWKRQWV NALEKGTRQL
     VPALVDVNNP GLTGAVQNQP DFQAGAADHR THFVSEVPAL VRQAMAEYST LTGRHYSPVH
     TYMCDDAEIV MVGLGSVCDD VEAVVDYLRS KGKKVGLVAI KLLQPFPEAE VVAALAGKKA
     VTVLERSDQT ALTTLVTQAL FKARENGEAK TVRHADIPAI KAIPRLTTAI FGLGGHDLQP
     RHLIAAFKAM ETGKSAPLVY LGSQFFSKTS NPRLAELQKR MKAAYPETEM MALEAEPNPR
     LLPDSAFRIR FHSVGGYGTI ASGKLLTDIL AGALDMQSKS APKYGSEKSG APTNYYITLS
     PQPIKITNAE LEDVEVVISP DHRSFVHTNP LKGLADGGTF ILQSSGTPEQ VWAELPAQFR
     KTIREKKINF FIIDAFAVAK RNAPTPELAT RMMGIAFIGA VAGHVKQVAG GASQKAILEK
     VRKQIQKKFG SKGDAVVAGN MQVIEEGIQA TQRVDYNAAA FTKIDAKPAP IVLRNVSLSS
     SMCQSSGSST CGLFDREYFS DMIATPFKEG TIGEAPVLPG TGLFMPAGSA GAKDKGLFRR
     TVPVFNAEVC TGCMECTLVC PDAAIPNTVH DIHELLATGI AQLDVTEAQR EAMRAQIIPM
     TEGIRETYRQ TKEERAFHEV VAEVAGKLPT KQATLLANFT KLVDVLAVYP VSKTRPFFDA
     MEKATPGTGG LFASTIDPWK CTGCLECVEV CGPGALSAQE QEPALLEMLQ TRFEFMSKTP
     NTPVRFFDTA LEGGEAKRLL LDRSNYYSTT GGHGGCRGCG EVTAIRQVMA TNHAITDKRK
     EAHIAELEET VAALEAKLAS LGKKDAARSQ RIDTALKALE KRLYLYEGGP TGNGPAGAII
     ANSTGCSSVY ASTFPFNAYN DPWVNSLFQD AQPLAKGIFE GIAAQALTDI RALRTAKLEL
     ADAYVPEQHD AEMRLLSSDK FTKEELALLP TIITVGGDGA TYDIGFGAFS RILASNTPIK
     VVVLNTGAYS NTGGQASTSS FIGQDSDLAR FGAAHSGKYE ARKELGLIAS FHSNVFVCST
     STALQGHFLK NTMEFLTYTD SPAVLDVYTP CQGEHGVADN VSAQQAALAV KSRMNPVFVH
     DPRRGKTLHD WFSLEGNPEP KATWSKQTLE YLDDKGELKL MTVPLTPASF ALTEIRFKKQ
     FRKLKADADN QMPVEQFIDL PEAQRKGKVP FVFATDGKKK LVKYGVSASI VALVEERRKH
     WQLLQYLDGQ HVSKMSDEYK KGIAALQSQV QESLKQRDAS LDGIARAMSE LAASSKAQVG
     NGVVIPIAPA GAAPAAAPAA AGAATAVATA IVTMEDSSKC TNCKTCYQDL SEIFEKTVMV
     VNGESREVAR IIPGALERVE VTPELKARIK RVSANCDAEI IR
//