ID A0A101GKC6_9BACT Unreviewed; 612 AA.
AC A0A101GKC6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:KUK60058.1};
GN ORFNames=XD81_0493 {ECO:0000313|EMBL:KUK60058.1};
OS Bacteroidetes bacterium 38_7.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1635292 {ECO:0000313|EMBL:KUK60058.1, ECO:0000313|Proteomes:UP000053999};
RN [1] {ECO:0000313|Proteomes:UP000053999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK60058.1}.
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DR EMBL; LGGC01000041; KUK60058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101GKC6; -.
DR PATRIC; fig|1635292.3.peg.268; -.
DR Proteomes; UP000053999; 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; 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 23..212
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 259..471
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 612 AA; 67237 MW; FCEAED05158273B9 CRC64;
MEENQNQTRV KDDIVIRFSG DSGDGMQLTG TLFSETAAFT GNDLSTFPDF PAEIRAPQNT
LAGVSGYQLH FGSTKIYNSG DLCDVLVAMN PASLKANLKW ARKGATIIID DDNFEDRAIQ
KAGYTSNPLT DGSLNSFVVI RVPMSRLTRE AVKDLGMDPK SADRSKNMFA LGILLYMFDK
PLEHTYHFIE KKFGKKPLVV EANKRVLRAG YDYADTVEIL HSRIHVQPAK MPKGRYRDIT
GNVATAWGLI AASEKSGRPL FLGSYPITPA SEILIELSKH RNLGVKTFQA EDEIAGINSA
IGASFAGSIG VTSTSGPGLS LKVEALGLAV MTELPLVVVD VQRAGPSTGM PTKPEQADLN
LALFGRNGEA PLIVMAASSP ADCFYTAFEA SKLSLEHMTP AILLSDGYIG LGSELFRIPK
MADLPEIKPP IAQPNTPYKP YARDQETLVR KWAIPGTEGL RHRIGGLEKT NIDGIVSTDP
INHETMVKLR AEKVKRIENF IPLQEVYGES KGRLLVVSWG GTYGAVRNAV DKCRSEGLKI
AHTHFKYLNP LPRNTAEILK AFDKVLVCEL NAGQFVNYLR MNFPEVKYAQ YNKIQGLPFM
VNELYEAIKS NF
//
