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Database: UniProt
Entry: L0JX84_9EURY
LinkDB: L0JX84_9EURY
Original site: L0JX84_9EURY 
ID   L0JX84_9EURY            Unreviewed;       660 AA.
AC   L0JX84;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:AGB36724.1};
GN   ORFNames=Natoc_0875 {ECO:0000313|EMBL:AGB36724.1};
OS   Natronococcus occultus SP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB36724.1, ECO:0000313|Proteomes:UP000010878};
RN   [1] {ECO:0000313|EMBL:AGB36724.1, ECO:0000313|Proteomes:UP000010878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP4 {ECO:0000313|EMBL:AGB36724.1,
RC   ECO:0000313|Proteomes:UP000010878};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA   Klenk H.-P.;
RT   "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003929; AGB36724.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0JX84; -.
DR   STRING; 694430.Natoc_0875; -.
DR   KEGG; nou:Natoc_0875; -.
DR   eggNOG; arCOG01606; Archaea.
DR   HOGENOM; CLU_017038_1_0_2; -.
DR   Proteomes; UP000010878; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010878}.
FT   DOMAIN          41..226
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          261..498
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          537..612
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   COILED          504..531
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   660 AA;  72758 MW;  8825A938A30EB3F4 CRC64;
     MAIYSKGFRH GETKIRIRLA TWPLISMSDD ELIWRVSGGS GDGIDSTSQN FAKALMRSGL
     DVFTHRHYPS RIRGGHTYVE IRAAADEVQS RGDGYNFLLA LGDSFARNPQ EEAYYGNEEI
     KPLSENLDEL REGGVIVYDE GLLSEDDVEE LELEERAEEN DWHVYPVDLR GLAKEHGREV
     MRNTAGIGVT AALLDMDLEH IEDLMSDAMG GDVLESNLEI LHEAYEMVDD DFETTHDLRA
     PEGDHDTEQA LLSGSNAIAY GAIDAGCRFI AGYPMTPWTD VFTILSQNFP DMGGVSEQVE
     DEIAAAALAV GASHAGVKAM SGSSGGGFAL MSEPLGLAEM TETPVVLIES MRAGPSTGMP
     TKPEQADLEH VLYTSQGDSQ RVVFAPGNIE EAYEQTRLAF DIAWDYQIPA IVIYDQKLSG
     ENKNVDVDFF DREPSPDLGS TLTEEELKEA AHDASGKFKR FDYKEATDGV ASRSIPGQKG
     GRYLATGNEH SPVGHISEDP DNRVFQMERR LEKLEQIRAE LDEERDSTQT YFGPEEADYG
     IITWGSSQGA VEEAIERLNE QGHSVKGISV SDMMPFAETE VTEFLESVDE AMVVEMNATA
     QFRGLIQKEL GRFGDKMTSL LKFNGNPFEP AEIVEGYEVN LADEDRQPEA QVRIEPAAGD
//
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