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Database: UniProt
Entry: A0A3M0I2P4_9ACTN
LinkDB: A0A3M0I2P4_9ACTN
Original site: A0A3M0I2P4_9ACTN 
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
//
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