ID D3RX49_FERPA Unreviewed; 391 AA.
AC D3RX49;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:ADC65062.1};
GN OrderedLocusNames=Ferp_0894 {ECO:0000313|EMBL:ADC65062.1};
OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Ferroglobus.
OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC65062.1, ECO:0000313|Proteomes:UP000002613};
RN [1] {ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D.,
RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.;
RT "Complete sequence of Ferroglobus placidus DSM 10642.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADC65062.1, ECO:0000313|Proteomes:UP000002613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613};
RX PubMed=22180810; DOI=10.4056/sigs.2225018;
RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A.,
RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T.,
RA Lovley D., Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Ferroglobus placidus AEDII12DO.";
RL Stand. Genomic Sci. 5:50-60(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; CP001899; ADC65062.1; -; Genomic_DNA.
DR RefSeq; WP_012965405.1; NC_013849.1.
DR AlphaFoldDB; D3RX49; -.
DR STRING; 589924.Ferp_0894; -.
DR PaxDb; 589924-Ferp_0894; -.
DR GeneID; 8778401; -.
DR KEGG; fpl:Ferp_0894; -.
DR eggNOG; arCOG01608; Archaea.
DR HOGENOM; CLU_002569_5_0_2; -.
DR OrthoDB; 372068at2157; -.
DR Proteomes; UP000002613; 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 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:ADC65062.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002613}.
FT DOMAIN 14..237
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 260..362
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 391 AA; 43267 MW; 13336598D619D65D CRC64;
MRRVVRGFYA IAEAVRLCRP NVICAYPITP QTEIVENLAE MYANGELDAE YITAESEFAA
ASIVLGASAA GARVFTATSS QGLLLMTEVL FNAAGMRLPI VMVVANRSVS APLSIWNDHQ
DSMTVRDAGI IQMHAENNQE AHDLIPLAYK VAEDKRVLLP FILNVDGFKL THAYEPVDLL
SQEVVDSFLP PYDPVVKLST EKPVAMGCYA PPPYYMEFRV AMEYAMERAK KVMEEAFKEW
SEIIGRDYGS HVSAEHCEDA EVVAIAMGSL VGLVRDVVEE MRKEGKKVGL LKIRTFRPFP
AEEVREALKN ANKVIIFERS LSIGSDPPVT LEVKSALFGS SSPEIHSVVI GLGGRDIPRE
QIVKVISEVY EGKVKPGKRY EGVKEFEEVI P
//