ID   A0A3A6QG47_9EURY        Unreviewed;       632 AA.
AC   A0A3A6QG47;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=2-oxoacid:acceptor oxidoreductase subunit alpha {ECO:0000313|EMBL:RJX45221.1};
GN   ORFNames=DM826_00560 {ECO:0000313|EMBL:RJX45221.1};
OS   Halonotius aquaticus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halonotius.
OX   NCBI_TaxID=2216978 {ECO:0000313|EMBL:RJX45221.1, ECO:0000313|Proteomes:UP000276588};
RN   [1] {ECO:0000313|EMBL:RJX45221.1, ECO:0000313|Proteomes:UP000276588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F13-13 {ECO:0000313|EMBL:RJX45221.1,
RC   ECO:0000313|Proteomes:UP000276588};
RA   Duran-Viseras A., Sanchez-Porro C., Ventosa A.;
RT   "Halonotius sp. F13-13 a new haloarchaeeon isolated from a solar saltern
RT   from Isla Cristina, Huelva, Spain.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RJX45221.1}.
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; QKNY01000001; RJX45221.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A6QG47; -.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000276588; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03710; OAFO_sf; 1.
DR   PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 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:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276588}.
FT   DOMAIN          15..197
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          237..478
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          509..582
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   632 AA;  68699 MW;  E2685681E8E02E8B CRC64;
     MTDNEFIWRI AGGSGDGIAS TSQNFAKALM RSGLDVFTHR HYPSRIRGGH TYTEVRAAAE
     PVKSRGDGYN FLLALGDSFA RNPQEDAYYG NEEIKPLSEN LDELREGGVI VYDSGLLDAS
     EIEDFDARVE ENNWHVYDID LRNMARDVGR EVMRNTAGVG VTCALAGIDL HWIEELMSDA
     MPEKILEPNL EILNKAHDMV VEEYDVDAND VTVPEGSHDE EQVLMSGSDA IAYGSLDEGC
     RFIAGYPMTP WTEVFTIMCQ NLPEVGGISE QVEDEIAAAA LAVGASHAGA KAMSGSSGGG
     FALMSEPLGL AEMTETPVVL IEAMRAGPST GMPTKPEQAD LEHVLYTSQG DSQRVVFAPG
     TVEEAYTQTR RAFQIAYEYQ IPAIVLYDQK LGGELVSLPA SHFDEEPNPS LGSTLTEAEL
     EEAPHDDSGK YSRFQHDVED GVSPRSIPGQ KGGRFLATGN EHTPEGHIAE TTSNRVAQMD
     RRTEKLEAIS ADLAAQDETH QTHYGPDEAT YGLMTFGSQQ GTVEEAVDML NEQGHSVKAL
     GVSDMAPYPV DEVSEFIESV DEVLVVEMNA SAQFRGLTQK ELGKYGEKLS SLLKYNGNPF
     EPLDIVEGFK TTIIEGGELS SNKTKFVPAA GD
//