ID L1KPT9_9ACTN Unreviewed; 645 AA.
AC L1KPT9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:EKX62632.1};
GN ORFNames=STRIP9103_05948 {ECO:0000313|EMBL:EKX62632.1};
OS Streptomyces ipomoeae 91-03.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX62632.1, ECO:0000313|Proteomes:UP000010411};
RN [1] {ECO:0000313|EMBL:EKX62632.1, ECO:0000313|Proteomes:UP000010411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91-03 {ECO:0000313|EMBL:EKX62632.1,
RC ECO:0000313|Proteomes:UP000010411};
RA Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL Submitted (NOV-2012) 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:EKX62632.1}.
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DR EMBL; AEJC01000499; EKX62632.1; -; Genomic_DNA.
DR RefSeq; WP_009327587.1; NZ_AEJC01000499.1.
DR AlphaFoldDB; L1KPT9; -.
DR PATRIC; fig|698759.3.peg.6670; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000010411; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000010411}.
FT DOMAIN 47..234
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 289..500
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 544..627
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 645 AA; 69408 MW; E50F7881E20C9419 CRC64;
MTSQVSSPAE QADKAVLGEL REQRKAAGTK DVRRLDRVII RFAGDSGDGM QLTGDRFTSE
TASFGNDLST LPNFPAEIRA PAGTLPGVSS FQLHFADHDI LTPGDAPNVL VAMNPAALKA
NIGDVPRGAE IIVNTDEFTK RAMQKVGYAA SPLEDGSLDG YSVHPVPLTT LTVEALKDFD
LSRKEAERSK NMFALGLLSW MYHRPTEGTE KFLKSKFAKK PDIAAANIAA FRAGWNFGET
TEDFAVSYEV APAATAFPVG TYRNISGNLA LSYGLIAASR QADLPLYLGS YPITPASDIL
HELSRHKNFG VRTFQAEDEI AGIGAALGAA FGGSLAVTTT SGPGVALKSE TIGLAVSLEL
PLLVIDIQRG GPSTGLPTKT EQADLLQAMF GRNGEAPVPV VAPRTPADCF DAALEAARIA
LTYRTPVLLL SDGYLANGSE PWRIPELDEL PDLTVQFAQG PNHTLDDGSE VFWPYKRDPQ
TLARPWAVPG TPGLEHRIGG IEKQDGTGNI SYDPANHDFM VRTRQAKIDG IDVPDVEVDD
PDGARTLVLG WGSTYGPITA AVRRLRTAGE YIAQAHLRHL NPFPRNLGAV LERYEKVVIP
EMNLGQLAML IRAKYLVDAH SYNQVNGMPF KAEQLAKALK EAIDG
//