ID A0A2H5B308_9ACTN Unreviewed; 613 AA.
AC A0A2H5B308;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:AUG78789.1};
GN ORFNames=CFP65_4022 {ECO:0000313|EMBL:AUG78789.1};
OS Kitasatospora sp. MMS16-BH015.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=2018025 {ECO:0000313|EMBL:AUG78789.1, ECO:0000313|Proteomes:UP000239175};
RN [1] {ECO:0000313|EMBL:AUG78789.1, ECO:0000313|Proteomes:UP000239175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS16-BH015 {ECO:0000313|EMBL:AUG78789.1,
RC ECO:0000313|Proteomes:UP000239175};
RA Kim S.B., Yun B.-R.;
RT "Genome sequence of Kitasatospora sp. MMS16-BH015.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP025394; AUG78789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5B308; -.
DR KEGG; kit:CFP65_4022; -.
DR Proteomes; UP000239175; Chromosome.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000239175}.
FT DOMAIN 10..197
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 247..463
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
SQ SEQUENCE 613 AA; 65167 MW; 60992BD2339B1A7F CRC64;
MIIRFAGDSG DGMQLTGDRF TSETASFGND LSTLPNFPAE IRAPAGTLPG VSSFQLHFAD
HDILTPGDAP NVLVAMNPAA LKANLADLPR GAELIVNTDE FTKRALTKVG YDSDPLADGS
LDAYRLHAVP LTSLTVEALK ESGLARKDAE RAKNMFALGL LSWMYHRPTH STEAFLRQKF
ARKPAIAEAN ITAYRAGWNY GETTESFAVS YEVAPSTFPA GTYRNISGNL ALSYGLIAAA
QRSGLPLFLG SYPITPASDI LHELSKHKNF GVRTFQAEDE IAGIGAALGA AFGGALGVTT
TSGPGVALKS ETIGLAVSLE LPLLVVDIQR GGPSTGLPTK TEQADLLQAM FGRNGEAPVP
IVAPATAAEC FDAAIEAARI AVTYRTPVLL LSDGYLANGS EPWRVPNVAE LPVIEPGFAT
APNHVLPDGS EVFWPYKRDS QTLARPWAVP GTAGLEHRIG GIEKQDGTGN ISYDPANHQH
MVRTRRAKID GIAVRPVEVD DPTGDARVLV LGWGSTYGPI TAAVRRVRRE GGRIAQTHLR
NVNPFPANLG AVLRGYDRVI VPEMNLGQLA LLLRAEYLVD VESFTQVTGL PFKAEQLAGA
LTAALTDGAP DHA
//