ID A0A0T1SSN4_9ACTN Unreviewed; 645 AA.
AC A0A0T1SSN4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:KQX59227.1};
GN ORFNames=ASD33_02720 {ECO:0000313|EMBL:KQX59227.1};
OS Streptomyces sp. Root1304.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX59227.1, ECO:0000313|Proteomes:UP000051136};
RN [1] {ECO:0000313|Proteomes:UP000051136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX59227.1, ECO:0000313|Proteomes:UP000051136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1304 {ECO:0000313|EMBL:KQX59227.1,
RC ECO:0000313|Proteomes:UP000051136};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQX59227.1}.
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DR EMBL; LMEP01000001; KQX59227.1; -; Genomic_DNA.
DR RefSeq; WP_056552531.1; NZ_LMEP01000001.1.
DR AlphaFoldDB; A0A0T1SSN4; -.
DR STRING; 1736450.ASD33_02720; -.
DR Proteomes; UP000051136; 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:UP000051136}.
FT DOMAIN 47..234
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 289..501
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 544..615
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 69394 MW; B6E04DE61E2FAAC3 CRC64;
MTSQVSSEAG EALLGEQRSA PAKPHHGTEK EVRRLDRVII RFAGDSGDGM QLTGDRFTSE
TASFGNDLST LPNFPAEIRA PAGTLPGVSS FQLHFADHDI LTPGDAPNVL VAMNPAALRA
NIGDVPRGGE IIVNTDEFAK RAMAKVGYAT SPLEDGSLDG YRVHPVPLTT LTVEALKDFG
LSRKEAERSK NMFALGLLSW MYHRPTEGTE TFLRQKFAKK PAIAEANIVA FRAGWNFGET
TEDFAVSYEI APATRAFPTG TYRNISGNLA LSYGLVAASR QADLPLYLGS YPITPASDIL
HELSRHKNFG VRTFQAEDEI AGIGAALGAA FGGSLAVTTT SGPGVALKSE TIGLAVSLEL
PLLIVDIQRG GPSTGLPTKT EQADLLQAMY GRNGEAPVPV VAPRTPADCF DAAIEAARIA
LTYRTPVFLL SDGYLANGSE PWRIPDVDEL PDLRTRFATG PNHTLDDGTE VFWPYKRDPE
TLARPWAVPG TPGLEHRIGG IEKQDGTGNI SYDPANHEFM VRTRQAKIDG IDVPDIEVDD
PDGAATLVLG WGSTYGPITA AVRRLRVAGH PIAQAHLRHL NPFPKNLGEV LERYEKVVVP
EMNLGQLATL VRAKYLVDAR SHTQVNGMPF KAEQLAAALK EAIDA
//
