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Database: UniProt
Entry: L0JQ15_NATP1
LinkDB: L0JQ15_NATP1
Original site: L0JQ15_NATP1 
ID   L0JQ15_NATP1            Unreviewed;       634 AA.
AC   L0JQ15;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:AGB32712.1};
DE   SubName: Full=Pyruvate flavodoxin/ferredoxin oxidoreductase domain protein {ECO:0000313|EMBL:ELY75923.1};
GN   OrderedLocusNames=Natpe_2915 {ECO:0000313|EMBL:AGB32712.1};
GN   ORFNames=C488_08687 {ECO:0000313|EMBL:ELY75923.1};
OS   Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / NCIMB
OS   786 / 157).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB32712.1, ECO:0000313|Proteomes:UP000010843};
RN   [1] {ECO:0000313|Proteomes:UP000010843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC   {ECO:0000313|Proteomes:UP000010843};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT   "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGB32712.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 15624 {ECO:0000313|EMBL:AGB32712.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT   "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000011593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 {ECO:0000313|Proteomes:UP000011593};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ELY75923.1, ECO:0000313|Proteomes:UP000011593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 {ECO:0000313|EMBL:ELY75923.1,
RC   ECO:0000313|Proteomes:UP000011593};
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).
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DR   EMBL; CP003372; AGB32712.1; -; Genomic_DNA.
DR   EMBL; AOIE01000061; ELY75923.1; -; Genomic_DNA.
DR   RefSeq; WP_006181103.1; NZ_AOIE01000061.1.
DR   AlphaFoldDB; L0JQ15; -.
DR   STRING; 797303.Natpe_2915; -.
DR   GeneID; 14333495; -.
DR   KEGG; npe:Natpe_2915; -.
DR   PATRIC; fig|797303.5.peg.1736; -.
DR   eggNOG; arCOG01606; Archaea.
DR   HOGENOM; CLU_017038_1_0_2; -.
DR   OrthoDB; 31112at2157; -.
DR   Proteomes; UP000010843; Chromosome.
DR   Proteomes; UP000011593; 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; 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   Pyruvate {ECO:0000313|EMBL:ELY75923.1}.
FT   DOMAIN          15..200
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          235..480
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          511..586
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   COILED          478..505
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   634 AA;  69728 MW;  76BF2B142FFBB571 CRC64;
     MSDDELIWRI AGGSGDGIDS TSQNFAKALM RSGLDVFTHR HYPSRIRGGH TYVEIRAADH
     EVQSRGDGYN FLLSLGDSFA RNPQEEAYYG NEEIKPLSEN LDELREGGII VYDEGLISEE
     DVEAIDLHER AEENDWHVFP MDLRGLAREH GREVMRNTAG VGVTAALLDM ELEHIEDLMS
     DAMGGDVLEA NLEILHEAYE TTREEYEFEH DLRAPEGSHD AEQALLSGSN AIAYGAIDAG
     CRFIAGYPMT PWTDVFTILA QNFPDMGGVS EQVEDEIAAA ALAVGASHAG VKAMSGSSGG
     GFALMSEPLG LAEMTETPVV LVESMRAGPS TGMPTKPEQA DLEHVLYTSQ GDSQRVVFAP
     GNIEEAYEQT RLAFDIAWDY QIPAIVIYDQ KLSGENTNVD VDFFDREVSP DLGSTLTEDE
     LREAAHDNSG KFKRFDYENA ENGVASRSIP GQKGGRFLAT GNEHSPVGHI SEDPDNRVAQ
     MDRRLEKLES IRAELDEERE STQTYFGDET ADYGIITWGS SQGAVEEAIE RLNANGHSVK
     GLSVSDMMPF PEKEVTEFLE SVDEAMVVEM NATAQFRGLL QKELGRFGEK LTSLLKYNGN
     PFEPAEIVEG YEVNLAEEDR EPTAQVRIEP AAGD
//
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