ID Q47LG5_THEFY Unreviewed; 617 AA.
AC Q47LG5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:AAZ56707.1};
GN OrderedLocusNames=Tfu_2674 {ECO:0000313|EMBL:AAZ56707.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56707.1};
RN [1] {ECO:0000313|EMBL:AAZ56707.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ56707.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000088; AAZ56707.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47LG5; -.
DR STRING; 269800.Tfu_2674; -.
DR KEGG; tfu:Tfu_2674; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR HOGENOM; CLU_017038_1_0_11; -.
DR OrthoDB; 9794954at2; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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 Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
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; IPR009014; Transketo_C/PFOR_II.
DR NCBIfam; TIGR03710; OAFO_sf; 1.
DR PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 20..207
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 258..474
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 617 AA; 66514 MW; 06B093CF7A2F7265 CRC64;
MPKEIQQLDR VIIRFAGDSG DGMQLTGDRF TQETASFGND LSTLPNFPAE IRAPAGTLPG
VSSFQLHFAD HDIMTPGDAP DVLVAMNPAA LKANLEDLPK GATIIVNTDE FTKRALAKVG
YTTNPLEDGS LADYKVSPVP LTSLTVKALE SFDISKKDAE RAKNMFALGL LSWMYNRPTE
GTLKFLQTKF AKKPEIMNAN IAAFKAGWNF GETTEDFAVS YEVKPAALPA GRYRNITGNL
ALSYGLIAAS KLSGLPLFLG SYPITPASDI LHELSKHKRF GVRTFQAEDE IAGVGAALGA
SFGGALGVTT TSGPGMALKA ETIGLAVMTE LPLVIIDVQR GGPSTGLPTK TEQADLLMAM
FGRNGESPLP VLAPRSPSDC FAIAIEAVRI ATKYRTPVIV LSDGYLANGS EPWRIPELSE
LPKLEVAFAR EPNGENGEFL PYLRDPETLA RPWAVPGTPG LEHRVGGIEK SDRTGEISYA
PANHDLMVRT RQAKIDGIAR DIEPLEVDDP TGDATVLALG WGGTYGSIAT AVRQVRRTGA
KIAHAHLRHL NPFPANLGEV LKRYERVVVP EINMGQLALL LRGRFLVDVI SYTKVRGLPF
KSDELAGVFQ EVIDRAE
//
