ID G6AH78_9BACT Unreviewed; 632 AA.
AC G6AH78;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9138_01455 {ECO:0000313|EMBL:EHG15879.1};
OS Prevotella histicola F0411.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=857291 {ECO:0000313|EMBL:EHG15879.1, ECO:0000313|Proteomes:UP000004597};
RN [1] {ECO:0000313|EMBL:EHG15879.1, ECO:0000313|Proteomes:UP000004597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0411 {ECO:0000313|EMBL:EHG15879.1,
RC ECO:0000313|Proteomes:UP000004597};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Mathney J.M.J., Dewhirst F.E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella histicola F0411.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHG15879.1}.
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DR EMBL; AFXP01000014; EHG15879.1; -; Genomic_DNA.
DR RefSeq; WP_008823366.1; NZ_JH376764.1.
DR AlphaFoldDB; G6AH78; -.
DR STRING; 857291.HMPREF9138_01455; -.
DR GeneID; 66730181; -.
DR PATRIC; fig|857291.3.peg.1451; -.
DR HOGENOM; CLU_017038_1_0_10; -.
DR Proteomes; UP000004597; Unassembled WGS sequence.
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; 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; 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; PF17147; PFOR_II; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004597}.
FT DOMAIN 22..212
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 257..453
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 514..579
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 632 AA; 69009 MW; D1D320DEFB5BA3C3 CRC64;
MEEQIEVKEL DNVVVHFSGD SGDGMQLAGN IFTTVSATVG NGVSTFPDYP ADIRAPQGSL
TGVSGFQVHI GAGKVYTPGD RCDVLVAMNA AALKMQYRHC KPNGTIIIDT DSFGQRDLQK
AEFRSDDYLG EMGIDPDRVV ACPITKMVKD CLADTGMDNK SMLKCRNMFA LGLVCWLFNR
DLTLVNNYLE KKFKKKPAIA EANIRVVQAG YDYGHNVHAS VPNTYRVESA VKEPGRYMDI
TGNKATAYGL MAAAERAGLR LFLGSYPITP ATDILHELAK HKSMGVTTVQ CEDEIAGCAS
AIGAAFAGAL AATSTSGPGI CLKSEAMNLA LIDELPLVIV DVQRGGPSTG MPTKSEQTDL
LQVLYGRNGE SPMPVIAATS PTDCFDAAYN ACKIALEHMT PVVLLTDAFI ANGSSAWKLP
NIEELPEIHP HFVTEEQKYK YTPYKRDPET LARYWAIPGT EGYTHILGGL EKDGETGSIS
TDPENHDKMD RLRWDKVARI PVPDLKVLGD EKDADLLIVG FGSSYGHLYS AMEELRAKGH
KVALAQFKYV NPLPKNTAEV LARYKKVVVA EQNLGQLAAL LRIRINHFAP YQYNQVKGQP
FVVSELVTAF EKLLKAPLPK EESGTFYTKI LQ
//
