ID F4HNR8_PYRSN Unreviewed; 395 AA.
AC F4HNR8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:AEC52212.1};
GN OrderedLocusNames=PNA2_1297 {ECO:0000313|EMBL:AEC52212.1};
OS Pyrococcus sp. (strain NA2).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=342949 {ECO:0000313|EMBL:AEC52212.1, ECO:0000313|Proteomes:UP000008293};
RN [1] {ECO:0000313|EMBL:AEC52212.1, ECO:0000313|Proteomes:UP000008293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2 {ECO:0000313|EMBL:AEC52212.1,
RC ECO:0000313|Proteomes:UP000008293};
RX PubMed=21602357; DOI=10.1128/JB.05150-11;
RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2,
RT isolated from a deep-sea hydrothermal vent area.";
RL J. Bacteriol. 193:3666-3667(2011).
CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain. {ECO:0000256|ARBA:ARBA00011595}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002670; AEC52212.1; -; Genomic_DNA.
DR RefSeq; WP_013748762.1; NC_015474.1.
DR AlphaFoldDB; F4HNR8; -.
DR STRING; 342949.PNA2_1297; -.
DR GeneID; 10554779; -.
DR KEGG; pyn:PNA2_1297; -.
DR PATRIC; fig|342949.8.peg.1302; -.
DR eggNOG; arCOG01608; Archaea.
DR HOGENOM; CLU_002569_5_0_2; -.
DR OrthoDB; 372068at2157; -.
DR Proteomes; UP000008293; Chromosome.
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 NCBIfam; NF040682; PorA_Arch; 1.
DR PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR32154:SF0; 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;
KW Pyruvate {ECO:0000313|EMBL:AEC52212.1}.
FT DOMAIN 16..239
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 262..362
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 395 AA; 43998 MW; 8837F7CFC3D77D99 CRC64;
MPIRTVMKAN EAAAWAAKLA KPKVIAAFPI TPSTLVPEKI SEFVANGELD AEFIKVESEH
SAISALVGAA AAGVRTFTAT ASQGLALMHE ILFIAAGMRL PIVMAIGNRA LSAPINIWND
WQDTISQRDT GWIQFYAENN QEALDLILLA YKVAENENVL LPAMVGFDAF ILTHTVEPVE
IPDQELVDEF LGEYEPKHAY LDPKRPITQG TLAFPAHYME ARYLVWEAME KAKKVIDEAF
AEFEKKFGRK YQKIEEYRTE DAEIIFVTMG SLAGTLKDWV DKKREEGYKV GAAKMTVYRP
FPVEEIRELA KKTKVLAFIE KDISMGLYGA VFTDASAALI NESEKPLMLD FIAGLGGRDV
TFGQLDEALK IAKEALEKGK VEKPIHWIGL RKELL
//