ID A0A0G0VW38_9BACT Unreviewed; 575 AA.
AC A0A0G0VW38;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:KKS05049.1};
GN ORFNames=UU56_C0001G0016 {ECO:0000313|EMBL:KKS05049.1};
OS Candidatus Curtissbacteria bacterium GW2011_GWA2_41_24.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1618411 {ECO:0000313|EMBL:KKS05049.1, ECO:0000313|Proteomes:UP000034493};
RN [1] {ECO:0000313|EMBL:KKS05049.1, ECO:0000313|Proteomes:UP000034493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKS05049.1}.
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DR EMBL; LCBC01000001; KKS05049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0VW38; -.
DR PATRIC; fig|1618411.3.peg.16; -.
DR Proteomes; UP000034493; 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 Pyruvate {ECO:0000313|EMBL:KKS05049.1}.
FT DOMAIN 15..180
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 211..380
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 477..567
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 575 AA; 62900 MW; DC2831D5EF7BF1CA CRC64;
MTPTEDFVWK VAGAAGEGIM TTGLLFSKTC ARHGWYIFDY TEYPSLIRGG HNTYQVAAGK
NPIYSQKEKV DLLIALNQDG IEQHQEEVGE NSLLVFDQEH QKIEIEKYNL AAKLIDLPMV
RLAKEAGGEE LMANNVALGA SVYLLGLDLD VLNQVIADVF ADKGQKVIAP NQQAARAGYN
FVKKQTQPQL SISKQSSNHL TMTGNEAVAL GAIAGGLQFY AAYPMTPSSS ILHYLAKNAH
TAKIVVKHAE DEISVINMAI GASFAGARAM VGTSGGGFCL MVEALGMAGI TELPIVIFEG
QRPGPALGLP TWTDQGDLKF VISASHGEFP RFVLVPGDAQ EAFEMTRKAL ILAETYQTPV
IILSDKYLAE SRFTINLATT TFTNGRFGIA ATPTADKTGF FPRYKLGDSP VSSRSLPGTA
GGVYIANSDD HDEYGLSSEE SSMRTNQVDK RNRKLELMRS EIPKQFWEEE PQSVLTFISF
GSTKGTIKSA REILTKEGIL TNHLNLSWLW PCPKEQIKQV LDNSKNTVVV EGNSEGQLVN
LIAQETGIII KNRLNRYDGR PFYPEEIVDY AKSSV
//
