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Database: UniProt
Entry: U3ACC7_9EURY
LinkDB: U3ACC7_9EURY
Original site: U3ACC7_9EURY 
ID   U3ACC7_9EURY            Unreviewed;       583 AA.
AC   U3ACC7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=2-oxoglutarate oxidoreductase, alpha subunit {ECO:0000313|EMBL:GAD52428.1};
GN   ORFNames=MBEHAL_1188 {ECO:0000313|EMBL:GAD52428.1};
OS   Halarchaeum acidiphilum MH1-52-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae.
OX   NCBI_TaxID=1261545 {ECO:0000313|EMBL:GAD52428.1, ECO:0000313|Proteomes:UP000016986};
RN   [1] {ECO:0000313|EMBL:GAD52428.1, ECO:0000313|Proteomes:UP000016986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16109 {ECO:0000313|EMBL:GAD52428.1,
RC   ECO:0000313|Proteomes:UP000016986};
RA   Shimane Y., Minegishi H., Nishi S., Echigo A., Shuto A., Konishi M.,
RA   Ito T., Ohkuma M., Ohta Y., Nagano Y., Tsubouchi T., Mori K., Usui K.,
RA   Kamekura M., Usami R., Takaki Y., Hatada Y.;
RT   "Whole genome sequencing of Halarchaeum acidiphilum strain MH1-52-1.";
RL   Submitted (SEP-2013) 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:GAD52428.1}.
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DR   EMBL; BATA01000022; GAD52428.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3ACC7; -.
DR   eggNOG; arCOG01606; Archaea.
DR   Proteomes; UP000016986; 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}.
FT   DOMAIN          13..177
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          213..458
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   REGION          442..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  63428 MW;  7BE62BCED1BD778E CRC64;
     MHDDLNWAIG GEAGDGIAST GKVFAQALSR AGRHVFTSKD FASRIRGGYT AYKVRTSVDR
     VQSVVDRLDV LIALTERTVD ENMDELHGDS VIIYDGERTE FSDFEVPEGM IGLDVPLKSL
     AEDAGGALMR NIVALGAVCE VAEFPIENLD ESLQKRFGSK GEKIVENNKE AARLGAEYVT
     ENYADAVGTL DYELETTDND YVLLNGDEAI GMGAIAAGCK FYAGYPITPA TDVMTYLTGR
     IEEFGGHVVQ AEDELSAINL ALGAARAGAR SMTATSGPGI DLMSETFGLV AQSETPLVIA
     DVMRSGPSTG MPTKQEQGDL NMLLYGGHGE IPRFVLAPTT VADCFHKTVE AFNLAEKYQT
     PVYIAADLAM AVTEQTFAPE EFDMDAVEID RGKVVDETEI SAWQNEKEQF KPHAVTADGV
     SPRAFPGTEG GVHMSTGLEH DELGRRTEDE EERIEQVDKR DQKVTTAEET EDWSPFEYGD
     EDADTLVISW GSNEGALVEA LDFLEEDGVD VRVLSVPYIF PRPDLSEDVA DAETTVVVEC
     NATGQFADVI ESDVLERVDR INKYNGVRFK ADELADDIKE VIA
//
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