ID B8CZW5_HALOH Unreviewed; 392 AA.
AC B8CZW5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase, alpha subunit {ECO:0000313|EMBL:ACL70817.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:ACL70817.1};
GN OrderedLocusNames=Hore_20720 {ECO:0000313|EMBL:ACL70817.1};
OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae;
OC Halothermothrix.
OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL70817.1, ECO:0000313|Proteomes:UP000000719};
RN [1] {ECO:0000313|EMBL:ACL70817.1, ECO:0000313|Proteomes:UP000000719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719};
RX PubMed=19145256; DOI=10.1371/journal.pone.0004192;
RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H.,
RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.;
RT "Genome analysis of the anaerobic thermohalophilic bacterium
RT Halothermothrix orenii.";
RL PLoS ONE 4:E4192-E4192(2009).
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DR EMBL; CP001098; ACL70817.1; -; Genomic_DNA.
DR RefSeq; WP_015923786.1; NC_011899.1.
DR AlphaFoldDB; B8CZW5; -.
DR STRING; 373903.Hore_20720; -.
DR KEGG; hor:Hore_20720; -.
DR eggNOG; COG0674; Bacteria.
DR HOGENOM; CLU_002569_5_0_9; -.
DR OMA; WNDQQDS; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000000719; Chromosome.
DR GO; GO:0019164; F:pyruvate 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 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; 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 Oxidoreductase {ECO:0000313|EMBL:ACL70817.1};
KW Pyruvate {ECO:0000313|EMBL:ACL70817.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000719}.
FT DOMAIN 16..239
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 262..366
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 392 AA; 43133 MW; 0265AF61BE0B9D17 CRC64;
MKPQIALTGN EALALGMRQI NPDVVAAYPI TPQTEVVQMF SQFVADGEVD TEFITVESEH
SAMSATVGAA AGGCRAMTAT SANGLALMWE IVYIAASLRL PIVMPLINRA LSAPINIHCD
HSDAMGVRDS GWIQLFGENA QQAYDNLIQA VRIAEHKNVR LPVIVNMDGF IISHAVENLK
PLTDQEVTDF IGDYKPEYSL LDPGNPITVG PLDLQDYYFE HKRQQIDGME HVFDVVAEVA
REFKELTGRE YGFFETYKMD DAEIAVLGLG STMGTARIAV DNLRADGIKA GLINLRLFRP
FPAGQLIRAL NGVKVLGVFD RADTFSLNGG PLFLDVKASL YDSSRDLKVV NYIYGLGGRD
INVSNIEDIL RELVAIKEGQ KEKKVTYYGV RE
//