ID   R4W3E2_9EURY            Unreviewed;       585 AA.
AC   R4W3E2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein {ECO:0000313|EMBL:AGN00477.1};
GN   ORFNames=L593_02630 {ECO:0000313|EMBL:AGN00477.1};
OS   Salinarchaeum sp. Harcht-Bsk1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Natronoarchaeaceae; Salinarchaeum.
OX   NCBI_TaxID=1333523 {ECO:0000313|EMBL:AGN00477.1, ECO:0000313|Proteomes:UP000014072};
RN   [1] {ECO:0000313|EMBL:AGN00477.1, ECO:0000313|Proteomes:UP000014072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Harcht-Bsk1 {ECO:0000313|EMBL:AGN00477.1};
RX   PubMed=23868130;
RA   Dominova I.N., Sorokin D.Y., Kublanov I.V., Patrushev M.V.,
RA   Toshchakov S.V.;
RT   "Complete Genome Sequence of Salinarchaeum sp. Strain HArcht-Bsk1T,
RT   Isolated from Hypersaline Lake Baskunchak, Russia.";
RL   Genome Announc. 1:E00505-13(2013).
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DR   EMBL; CP005962; AGN00477.1; -; Genomic_DNA.
DR   RefSeq; WP_020445371.1; NC_021313.1.
DR   AlphaFoldDB; R4W3E2; -.
DR   STRING; 1333523.L593_02630; -.
DR   GeneID; 16180453; -.
DR   KEGG; sali:L593_02630; -.
DR   PATRIC; fig|1333523.5.peg.533; -.
DR   eggNOG; arCOG01606; Archaea.
DR   HOGENOM; CLU_017038_1_0_2; -.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000014072; Chromosome.
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:AGN00477.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014072}.
FT   DOMAIN          13..175
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          207..452
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   REGION          422..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..473
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  63847 MW;  FFF8569ED801122D CRC64;
     MAEDLNWAIG GEAGDGIDST GKIFAQAQSR AGRHVFTSKD FASRIRGGYT AYKIRSSTER
     VQSVVDRLDV LVALTQRTID ENLDELHDRS VVVYDGERSW EAEIPGEIDA VDVPLKSLAE
     EAGGAIMRNV VALGAVCAIV DFPVEKLDEA LEKRFGGKGE KIVENNKQAA RLGAEYVEEN
     YDGFDYSLET TDNDYVLLNG DEAIGMGAIA AGCRFYAGYP ITPATDVMEY LTGRIDRFGG
     HVVQAEDELS AINMALGAAR AGARSMTATS GPGIDLMTET FGLVATSETP LVICDVMRAG
     PSTGMPTKQE QGDLNMLLYG GHGEIPRFVV APTTIAECFH KTVEAFNLAE KYQTPVYLVS
     DLALAVTEQT FAPEEFDMDA VEIDRGNVVD EDSIDEYLDE QGRFQPHYDA ADGVSPRAFP
     GTTAGAHMST GLEHDELGRR TEDTEERIDQ VEKRQRKVET AQNEEDWSPR EFGDPDADTL
     VLSWGSNEGA IVEAMDHLET EENLSVRFLS VPYMFPRPDL SDAIEAAEET VVVECNANGQ
     FADVVEHDVL TRVERVTKFD GVRFDADELA DAIRDVAADA DEVTA
//