ID   A0A256IDG5_9EURY        Unreviewed;       587 AA.
AC   A0A256IDG5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Oxoglutarate--ferredoxin oxidoreductase {ECO:0000313|EMBL:OYR54570.1};
GN   ORFNames=DJ70_13665 {ECO:0000313|EMBL:OYR54570.1};
OS   Halorubrum halodurans.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=1383851 {ECO:0000313|EMBL:OYR54570.1, ECO:0000313|Proteomes:UP000216308};
RN   [1] {ECO:0000313|EMBL:OYR54570.1, ECO:0000313|Proteomes:UP000216308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cb34 {ECO:0000313|EMBL:OYR54570.1,
RC   ECO:0000313|Proteomes:UP000216308};
RX   PubMed=24782836; DOI=10.3389/fmicb.2014.00140;
RA   Fullmer M.S., Soucy S.M., Swithers K.S., Makkay A.M., Wheeler R.,
RA   Ventosa A., Gogarten J.P., Papke R.T.;
RT   "Population and genomic analysis of the genus Halorubrum.";
RL   Front. Microbiol. 5:140-140(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:OYR54570.1}.
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DR   EMBL; NHPJ01000118; OYR54570.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256IDG5; -.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000216308; 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   Reference proteome {ECO:0000313|Proteomes:UP000216308}.
FT   DOMAIN          13..176
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          210..455
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   REGION          431..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   587 AA;  64173 MW;  AAA02B27F9D50CE0 CRC64;
     MAADFNWAVG GEAGDGIDST GKIFAQALSR SGRHVFTSKD FASRIRGGYT AYKVRTSVDK
     VQSVVDRLDV LIALTPRTIE ENLEELHEGS VIIYDGERTT MQNVEIPEGM IGIDVPLKRL
     AEEAGGAIMR NVVALGAACE VAEFPIENLD SALEKRFGDK GQKLVDNNKE AARAGRSYVA
     EEYDAEFEYD LETTDEDYVL LNGDEAIGMG AIAAGCRFYS GYPITPATDV MTYLTGRLER
     YGGHVVQAED ELSAINMALG AARGGARAMT ATSGPGIDLM TETFGLVATS ETPLVICNVM
     RSGPSTGMPT KQEQGDLNHM LYGGHGEVPR FVLAPTTVDE CFWKTVEAFN LAEKYQLPVY
     LTADLSMAVT EQTFSPDAFD MDAVEVDRGF VVDDASVDEH LSESGGFKPH ELTEDGVSPR
     AFPGTVDGAH MSTGLEHDEQ GRRTEDTEMR VEQVDKRNRK VETAEDREDW SPREFGDADA
     ENLVITWGSN EGALAEALDM LEADDIDIRV LSVPYVFPRP DLTEEIEAAD ETIVVECNET
     GQFANLIERD ALVRVDRINK YDGVRFKADE LAREIKATLE TGTEATQ
//