ID   M0NQT1_9EURY            Unreviewed;       631 AA.
AC   M0NQT1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:EMA60307.1};
GN   ORFNames=C468_13361 {ECO:0000313|EMBL:EMA60307.1};
OS   Halorubrum kocurii JCM 14978.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1230456 {ECO:0000313|EMBL:EMA60307.1, ECO:0000313|Proteomes:UP000011546};
RN   [1] {ECO:0000313|EMBL:EMA60307.1, ECO:0000313|Proteomes:UP000011546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14978 {ECO:0000313|EMBL:EMA60307.1,
RC   ECO:0000313|Proteomes:UP000011546};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA60307.1}.
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; AOJH01000081; EMA60307.1; -; Genomic_DNA.
DR   RefSeq; WP_008849345.1; NZ_AOJH01000081.1.
DR   AlphaFoldDB; M0NQT1; -.
DR   STRING; 1230456.C468_13361; -.
DR   PATRIC; fig|1230456.3.peg.2655; -.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000011546; 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   Pyruvate {ECO:0000313|EMBL:EMA60307.1}.
FT   DOMAIN          15..198
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          234..478
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          507..578
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   REGION          399..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  68438 MW;  4E9C1B6264069775 CRC64;
     MTDDELIWRI SGGSGDGIAS TSQNFAKALM RSGLNVFTHR HYPSRIRGGH TYTEVRASAD
     PVESRGDGYN FLLALGDSFA RNPQEKSVYG NEEIKPLSEN LDELREGGVI VYDEGLLDAS
     EIPDFEERAE ENDWHVFPLD LRGLARDMGR EVMRNTAGVG ATCALTGMDL NHVEDLMRDA
     MPEKILEPNL EILETAYDQV REEYDVDAPD VSVPTGEHDE TQLLMSGSDA ISYGAIDEGC
     RFIAGYPMTP WTEVFTIMTQ NLPELGGISE QVEDEIAAAA LAVGASHAGV KAMSGSSGGG
     FALMSEPLGL AEMTETPVVL VEAMRAGPST GMPTKPEQSD LEHVLYTSQG DSQRVVLAPG
     TVEEAYEQSR IAFRLAYEYQ IPAILLYDQK LGGEMTNVPK SHFDREPNPT LGKTLSEDAL
     ADEPHSTDGK FHRFQHDVED GVSPRSIPGQ KGGRFLATGN EHSPTGHIEE SPDNRVAQID
     RRTQKLEAIR ADLDTEDTGS YAGPEDAQYG ILTFGSQQGT VEEAVGRLND AGVSVKSYGV
     SDMLPFPTEQ VEAFIESVDE VLVVEMTASG QFRGLVQKNL GRYGERLSSL LKYNGNPFEP
     AEVVDGFEAA IIEGDGDASG HQTTFVPAAG D
//