ID A0A0T6AAU6_9BACT Unreviewed; 623 AA.
AC A0A0T6AAU6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein {ECO:0000313|EMBL:KRT72196.1};
DE EC=1.2.7.3 {ECO:0000313|EMBL:KRT72196.1};
GN ORFNames=XU13_C0028G0006 {ECO:0000313|EMBL:KRT72196.1};
OS Candidatus Rokubacteria bacterium CSP1-6.
OC Bacteria; Candidatus Rokubacteria.
OX NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT72196.1, ECO:0000313|Proteomes:UP000051916};
RN [1] {ECO:0000313|EMBL:KRT72196.1, ECO:0000313|Proteomes:UP000051916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT72196.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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:KRT72196.1}.
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DR EMBL; LDXP01000028; KRT72196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6AAU6; -.
DR STRING; 1640509.XU13_C0028G0006; -.
DR PATRIC; fig|1640509.3.peg.1445; -.
DR Proteomes; UP000051916; Unassembled WGS sequence.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:KRT72196.1}; Pyruvate {ECO:0000313|EMBL:KRT72196.1}.
FT DOMAIN 30..219
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 268..479
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 623 AA; 67587 MW; B982CBA9DA26E167 CRC64;
MSDAVASPAT AAKPRRQLDR AVVRFAGDSG DGMQVTGEQF ATEAAWAGAD LVTLPNFPAE
IRAPAGTLFG VSSYQLQFGS RRVYTPGDRL DCLVAMNPAA LKVHQRDLKD GGLLIVNTAA
FEKKNLDRAG YTSNPLDDPA LEDRYRLHKV DITRLTMDAL ESVPLNVKEK ERCKNFFSLG
LVSWIYTRPI EPTVAWITKR FAKNPAFVEA NTRALKAGYH YGETAEIFTE CYGIEPAEMP
PGLYRSITGN RALAWGILAA AERTKLTVVY GAYPITPASD VLHEISLHKR FGVRAIQAED
EIAAVGTIIG AAFGGAIGVC ASSGPGIALK AEGVNLAVMA ELPIVIFDVQ RAGPSTGLPT
KTEQADLLMA LHGRNSESPV VVLAPMTPGD CFFVAYEAIR IAVKYMVPVI VLSDGYLASG
AEPWLIPDPK TLPDIPVSFR TNPEGFAPYV RDEATLARPW VRPGTAGLEH RIGGLEKENI
TGNVSYDADN HDLMVRLRAE KVRRVAQEIP PTTVNGPAAG DLLVVGWGST YGTITAAVEE
VQQSGKAVAS VHLRHLNPLP PDLGQILRQY ERILVPEINS GQLVRILRAE YLVDAVGFNR
VRGLPLSTEE LREAIEQLLK EKR
//
