ID H0BXW1_9BURK Unreviewed; 1061 AA.
AC H0BXW1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Pyruvate ferredoxin/flavodoxin oxidoreductase {ECO:0000313|EMBL:EHL22921.1};
GN ORFNames=KYG_11170 {ECO:0000313|EMBL:EHL22921.1};
OS Acidovorax sp. NO-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL22921.1, ECO:0000313|Proteomes:UP000003485};
RN [1] {ECO:0000313|EMBL:EHL22921.1, ECO:0000313|Proteomes:UP000003485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NO-1 {ECO:0000313|EMBL:EHL22921.1,
RC ECO:0000313|Proteomes:UP000003485};
RX PubMed=22374962; DOI=10.1128/JB.06814-11;
RA Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL J. Bacteriol. 194:1635-1636(2012).
CC -!- SIMILARITY: Belongs to the pyruvate:ferredoxin/flavodoxin
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009032}.
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DR EMBL; AGTS01000077; EHL22921.1; -; Genomic_DNA.
DR AlphaFoldDB; H0BXW1; -.
DR STRING; 512030.KYG_11170; -.
DR PATRIC; fig|512030.4.peg.2194; -.
DR Proteomes; UP000003485; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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 GO; GO:0022900; P:electron transport chain; IEA:InterPro.
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 Gene3D; 4.10.780.10; Pyruvate-flavodoxin oxidoreductase, EKR domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR037112; Pyrv-flavodox_OxR_EKR_sf.
DR InterPro; IPR019456; Pyrv-flavodox_OxRtase_EKR.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR011895; Pyrv_flavodox_OxRed.
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 NCBIfam; TIGR02176; pyruv_ox_red; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF10371; EKR; 1.
DR Pfam; PF12838; Fer4_7; 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 SMART; SM00890; EKR; 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; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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:EHL22921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003485};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 693..722
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 750..780
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1061 AA; 114317 MW; 8588A4D5AD15F9EE CRC64;
MNDMHTSQGD RRTLDANEAV ASVAYRASEV IAIYPITPAS AMGELADVWA ADHKPNLSGS
VPKVVEMQSE GGAAGAVHGA LQAGALVTTF TASQGLLLML PDMYKIAGEL TSFCMHVAAR
SVATHALSIF GDHSDVMAAR GTGFALLASG SAQEAQDLAA VGHAVTLKVR IPVLHFFDGF
RTSHEIGTVA VLDDQTLRAL LPANGIAAHR QRALDPERPV IRGTSQNPDT FFQGREAVEP
FYTAFPEALE ATFSHFAALT GRQYHLFDYV GDPAAERVIV LMGSGAECAH EVVEHLVAQG
ERVGAVKVRL FRPFSVEHLL QALPTTVQAI AVLDRTKEPG SSGEPLLQEV TTGLVQAVAD
GRRTALPRIS GGRYGLAGKE FTPAMVKAVF DALALPRPPA RFTVGIRDDV SGSSLAWDSA
FDRELEAPDV MRAVFFGLGS DGTVSANKAS IKLIGEQAGL FAQGYFELDS RKAGSTTVSH
LRFGPRPIHS TYRITQAQFV AIHAPEFLER RDVLNIAAPG ATVLLNTEVP AARVWDTLPS
EVQQQLIQRR CRLYAIDGYA QAERAGLGRR INTVMQLCFF ALSKVLPMDE AMVHLRRSLE
EHWGRRGPEV VRRNLLALEG TLEALTEIAV PEQATATRAR PSAVPVQAAD FIQRVTRLLL
EGRGDELPVS AFPPDGTWPS GTSRWEKRAI ALDIPIWQPD LCVQCNRCVT ICPHAAIRAK
VYDPAALGDA PAGFPSLMEA FEPSLEGLAY TVQVAPEDCT GCGLCIEVCP AKDRHDTRRR
ALVSKPLVEH RAVQRAAFDY FEQIPLAELR HLPLEPRNVA FRQPLFEFSG ACAGCGETPY
LRLLTQLFGD RLLVANATGC SSIYGGNLPT TPWTVNAQGR GPAWSNSLFE DNAEFGLGMR
LALDAATDRA RALLESLAPR LPAELVAGLL QPPDREGTGE TWALAQRQRV SELEHLLAQD
TSPEATALRD AAPALLPRSV WIVGGDGWAY DIGYGGLDHV LASHHKVNVL VLDTEVYSNT
GGQQSKATPL GASAKFAIAG KAVRKKDLGL LAMGYGHVYV A
//
