ID A0A0P9DVK7_9ARCH Unreviewed; 354 AA.
AC A0A0P9DVK7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Ketoisovalerate oxidoreductase subunit VorB {ECO:0000313|EMBL:KPV64156.1};
GN Name=vorB {ECO:0000313|EMBL:KPV64156.1};
GN ORFNames=AOA65_1041 {ECO:0000313|EMBL:KPV64156.1};
OS Candidatus Bathyarchaeota archaeon BA1.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV64156.1, ECO:0000313|Proteomes:UP000050312};
RN [1] {ECO:0000313|EMBL:KPV64156.1, ECO:0000313|Proteomes:UP000050312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA1 {ECO:0000313|EMBL:KPV64156.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(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:KPV64156.1}.
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DR EMBL; LIHJ01000041; KPV64156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9DVK7; -.
DR STRING; 1700835.AOA65_1041; -.
DR KEGG; barc:AOA65_1041; -.
DR PATRIC; fig|1700835.3.peg.1732; -.
DR Proteomes; UP000050312; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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 InterPro; IPR033412; PFOR_II.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR43088; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR43088:SF1; SUBUNIT OF PYRUVATE:FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
FT DOMAIN 15..235
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 248..341
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 354 AA; 38496 MW; CBEF103F6F961902 CRC64;
MTEKKFMTGN EAIAEAAIQA GCRCYFGYPI TPQNEICEYM SWRLPEVGGC FIQAESEVAA
IYMVFGAAGA GARVMTSSSS PGISLMMEGI SYIAAAELPC VMVNIMRGGP GLGGIQPSQS
DYFQATKGGG HGDYHMLVLA PSTVQEAVNL TMLAFDLADK YCNPVMILGD GYIGQVMEPV
EFKPTEKSFV VPRKEWAITG ASGRPRNLIK TLYLDPAVLE ERNLHIARKL QEAVKNEVSV
ETHATEDAEI IIAAYGTVAR ITKTAIKILR EKGLKVGLIR PISLYPFPYQ TFAQVSEKVK
HFLVVEMSLG QMVEDVKLAI GDKSQVHFYG RVGGMVPTYD EMVAEVEKIA GEAG
//
