ID A0A0K9XBM3_9ACTN Unreviewed; 661 AA.
AC A0A0K9XBM3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KNB50057.1};
GN ORFNames=AC230_25440 {ECO:0000313|EMBL:KNB50057.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB50057.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
RL Submitted (JUL-2015) 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:KNB50057.1}.
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DR EMBL; LFXA01000017; KNB50057.1; -; Genomic_DNA.
DR RefSeq; WP_049718603.1; NZ_LFXA01000017.1.
DR AlphaFoldDB; A0A0K9XBM3; -.
DR STRING; 1678637.AC230_25440; -.
DR PATRIC; fig|1678637.3.peg.5435; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000037288; 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:UP000037288}.
FT DOMAIN 62..249
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 304..519
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 560..625
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 70998 MW; BE4625240AC61F8F CRC64;
MTSQVSSPAE QADSAEQPGF SPPDTGDEPS RLAGQRGSAP RSDGKEVRRL DRVIIRFAGD
SGDGMQLTGD RFTSETASFG NDLSTLPNFP AEIRAPAGTL PGVSSFQLHF ADHDILTPGD
APNVLVAMNP AALKANLGDL PRGAEIIVNT DEFTKRPMAK VGYDTSPLED GSLDAYSVHP
VPLTTLTLEA LKEFGLPRKE AERSKNMFAL GLLSWMYHRP TENTEAFLRR KFAGKPQIAE
ANVAAFRAGW NFGETTEDFA VSYEVAPATA AFPPGSYRNI SGNLALAYGL IAAGQQADLP
LYLGSYPITP ASDILHELSK HKNFGVRTFQ AEDEIAGIGA ALGAAFGGAL AVTTTSGPGV
ALKSETIGLA VSLELPLLVV DIQRGGPSTG LPTKTEQADL LQAMYGRNGE APVPVVAPKT
PADCFAAALD AARIALAYRT PVFLLSDGYL ANGSEPWRIP EPDELPDLRV QFATTPNHTL
ADGTEVFWPY KRDPHTLARP WAVPGTPGLE HRIGGIEKQD GTGNISYDPA NHDHMVRTRQ
AKIDNITVPD TEVDDPSGQA RTLILGWGST YGPITAAVRR VRNQGHHVAQ AHLRHLNPFP
RNLGEVLRRY DTVVVPEMNL GQLATLLRAR YLVDIHSHTQ VSGMPFKAEQ LATVIEEAID
V
//
