ID A0A3M0I2P4_9ACTN Unreviewed; 642 AA.
AC A0A3M0I2P4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit alpha {ECO:0000313|EMBL:RMB80349.1};
GN ORFNames=CTZ28_41045 {ECO:0000313|EMBL:RMB80349.1};
OS Streptomyces shenzhenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943815 {ECO:0000313|EMBL:RMB80349.1, ECO:0000313|Proteomes:UP000270471};
RN [1] {ECO:0000313|EMBL:RMB80349.1, ECO:0000313|Proteomes:UP000270471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=193 {ECO:0000313|EMBL:RMB80349.1,
RC ECO:0000313|Proteomes:UP000270471};
RA Siqueira K.A., Liotti R.G., Mendes T.A.O., Soares M.A.;
RT "Draft genome of actinobacteria isolated from guarana (Paullinia cupana
RT (Mart.) Ducke.";
RL Submitted (NOV-2017) 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:RMB80349.1}.
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DR EMBL; PENI01000044; RMB80349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0I2P4; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000270471; 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:UP000270471}.
FT DOMAIN 44..231
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 284..494
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 541..612
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 68950 MW; 5ECF4C01F0DA1F4F CRC64;
MTSQVSSPAE QADGTVVGEQ RRPDGTKDVR RLDRVVIRFA GDSGDGMQLT GDRFTSETAS
FGNDLSTLPN FPAEIRAPAG TLPGVSSFQL HFADHDILTP GDAPNVLVAM NPAALKANIG
DLPRGAEIIV NTDEFTKRAM QKVGYATSPL EDGSLAGYGL HPVPLTTLTV EALKDFDLTR
KEAERSKNMF ALGLLSWMYH RPTEGTERFL RSKFAKKPEI AEANLTAFRA GWNFGETTED
FAVSYEVAPA TKAFPVGTYR NISGNLALAY GLVSASRQAD LPLFLGSYPI TPASDILHEL
SKHKNFGVRT FQAEDEIAGI GAALGAAFGG SLAVTTTSGP GVALKSETIG LAVSLELPLL
VIDIQRGGPS TGLPTKTEQA DLLQAMFGRN GEAPVPIVAP RTPGDCFDAA LEAARIALTY
RTPVLLLSDG YLANGSEPWR IPALEELPDL RVRFAQGPNH TLDDGTEVFW PYKRDPQTLA
RPWAVPGTPG LEHRIGGIEK QDGTGNISYD PANHDFMVRT RQAKIDGIEV PDIEVDDPDG
ASLLVLGWGS TFGPITAAVR RLRVQGVPVA QAHLRHLNPF PGNLGEVLGR YEKVVVPEMN
LGQLALLIRA KYLVDARSYN QVSGMPFKAE QLAAALKEAI DA
//