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Database: UniProt
Entry: F4HNR8_PYRSN
LinkDB: F4HNR8_PYRSN
Original site: F4HNR8_PYRSN 
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}.
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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
//
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