ID A0A238UP63_HALVU Unreviewed; 631 AA.
AC A0A238UP63;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase alpha subunit {ECO:0000313|EMBL:SNR23089.1};
GN ORFNames=SAMN06264855_10158 {ECO:0000313|EMBL:SNR23089.1};
OS Halorubrum vacuolatum (Natronobacterium vacuolatum).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=63740 {ECO:0000313|EMBL:SNR23089.1, ECO:0000313|Proteomes:UP000198397};
RN [1] {ECO:0000313|EMBL:SNR23089.1, ECO:0000313|Proteomes:UP000198397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8800 {ECO:0000313|EMBL:SNR23089.1,
RC ECO:0000313|Proteomes:UP000198397};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FZNQ01000001; SNR23089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238UP63; -.
DR OrthoDB; 31112at2157; -.
DR Proteomes; UP000198397; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:SNR23089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198397}.
FT DOMAIN 15..198
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 234..478
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 507..581
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 440..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 68710 MW; 4C852EE1FD6BCF73 CRC64;
MTDEELIWRI SGGSGDGIAS TSQNFAKALM RSGLNVFTHR HYPSRIRGGH TYTEIRAAAE
PVKSRGDGYN FLLALGDSFA RNPQEEALYG NEEIKPLSEN LDELREGGVI VYDAGLLDTS
EIPDFDERAE ENGWHVYPLD LRGLAREQGR EVMRNTAGVG ATCALIGMEL SYVEELMRDA
MPEKILDPNL EILNIAYEQV IDEHDVDAHD VQIPTGEHES DQLLMSGSDA IAYGAIDEGC
RFIAGYPMTP WTEVFTIMSQ NLPKLGGISE QVEDEIAAAA LAVGASHAGV KAMSGSSGGG
FALMSEPLGL AEMTETPVVL LEAMRAGPST GMPTKPEQSD LEHVLYTSQG DSQRVVLAPG
TVEEAYEQSR LAFRIAYEYQ IPVVLLYDQK LGGELMNVPR DAFDREPNPE LYHTLTEEEL
PEQPHSADGK FHRYQHDVEN GVSPRSLPGQ QGGRYLASGN EHDPTGHISE SPDNRVAQID
RRAEKLAAIR ADLDTESTQS HHGPEEADYG IMTFGSQQGT VEEAVDVLNA AGHSVKSLGV
SDMLPFPSEE VEAFIESVDE VLVVEMTASG QFRGLVQKNL GRHGEKLSSL LKYNGNPFEP
AEIVDGFEAV IIEDGTDDPA HQTTFVPAAG D
//