ID   M0PHY4_9EURY            Unreviewed;       585 AA.
AC   M0PHY4;
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-containing protein {ECO:0000313|EMBL:EMA69498.1};
GN   ORFNames=C461_02681 {ECO:0000313|EMBL:EMA69498.1};
OS   Halorubrum aidingense JCM 13560.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1230454 {ECO:0000313|EMBL:EMA69498.1, ECO:0000313|Proteomes:UP000011575};
RN   [1] {ECO:0000313|EMBL:EMA69498.1, ECO:0000313|Proteomes:UP000011575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13560 {ECO:0000313|EMBL:EMA69498.1,
RC   ECO:0000313|Proteomes:UP000011575};
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:EMA69498.1}.
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DR   EMBL; AOJI01000014; EMA69498.1; -; Genomic_DNA.
DR   RefSeq; WP_007998418.1; NZ_AOJI01000014.1.
DR   AlphaFoldDB; M0PHY4; -.
DR   STRING; 1230454.C461_02681; -.
DR   PATRIC; fig|1230454.4.peg.551; -.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000011575; 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; 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; 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:EMA69498.1}.
FT   DOMAIN          13..175
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          210..454
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   REGION          426..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  64001 MW;  01389812E9BFC6BC CRC64;
     MAADFNWAVG GEAGDGIDST GKIFAQALSR AGRHVFTSKD FASRIRGGYT AYKVRTSVDK
     VQSVVDRLDV LIALTPRTIE ENLDELHEGS VIIYDGERTT MQDVEIPDEM IGIDVPLKRL
     AEEAGGAIMR NVVALGAACE VAEFPIENLD SALEKRFKDK GQKLVDNNKE AARAGQSFVA
     EEYDHEFDYD LETTDEDYVL LNGDEAIGMG AIAAGCRFYA GYPITPATDV MTYLTGRIER
     YGGHVVQAED ELSAINMALG AARGGARSMT ATSGPGIDLM TETFGLIATS ETPLVICNVM
     RSGPSTGMPT KQEQGDLNQM LYGGHGEVPR FVLAPTTIAE CFWKTVEAFN LAEKYQLPVY
     LTADLSMAVT EQTFTPDTFD MDEVEVDRGF VVDEADIDGH MSESGGFQPH EITDDGISPR
     AFPGTADGAH MSTGLEHDEQ GRRTEDTDMR VAQVDKRNRK VETAREREDW GPREFGDEDA
     DALVITWGSN EGALAEAIDL LEEDDLAVRV LSVPYIFPRP DLTEDVEAAD DVIVVECNER
     GQFANLVEHD VLARVDRINK YNGVRFKADE LADEIKETLE AGVEA
//