ID   C9YXR3_STRSW            Unreviewed;       645 AA.
AC   C9YXR3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:CBG70842.1};
GN   OrderedLocusNames=SCAB_37561 {ECO:0000313|EMBL:CBG70842.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG70842.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG70842.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG70842.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN554889; CBG70842.1; -; Genomic_DNA.
DR   RefSeq; WP_013001470.1; NC_013929.1.
DR   AlphaFoldDB; C9YXR3; -.
DR   STRING; 680198.SCAB_37561; -.
DR   GeneID; 24310328; -.
DR   KEGG; scb:SCAB_37561; -.
DR   eggNOG; COG0674; Bacteria.
DR   eggNOG; COG1014; Bacteria.
DR   HOGENOM; CLU_017038_1_0_11; -.
DR   Proteomes; UP000001444; 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; 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:UP000001444}.
FT   DOMAIN          47..234
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          289..502
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          544..627
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  69378 MW;  7FA147BA1B86BDF2 CRC64;
     MTSQVSSPAE QADEAALGEL REQRKPAGTK DVRRLDRVII RFAGDSGDGM QLTGDRFTSE
     TASFGNDLST LPNFPAEIRA PAGTLPGVSS FQLHFADHDI LTPGDAPNVL VAMNPAALKA
     NLGDVPRGAE IIVNTDEFTK RAMQKVGYAT SPLEDGSMDG YSVHPVPLTA LTVEALKSFD
     LSRKEAERSK NMFALGLLSW MYHRPTEGTE KFLAAKFAKK PEIAAANLAA FRAGWNFGET
     TEDFAVSYEV APAAAAFPVG TYRNISGNLA LSYGLIAASR QADLPLYLGS YPITPASDIL
     HELSRHKNFG VRTFQAEDEI AGIGAALGAA FGGSLAVTTT SGPGVALKSE TIGLAVSLEL
     PLLVIDIQRG GPSTGLPTKT EQADLLQAMY GRNGEAPVPV VAPRTPADCF DAAIEAARIA
     LTYRTPVFLL SDGYLANGSE PWRIPETDEL PDLTVQFTQG PNHTLDDGTE VFWPYKRDPE
     TLARPWAIPG TPGLEHRIGG IEKQDGTGNI SYDPANHDFM VRTRQAKIDG IDVPDVEVDD
     PHEARTLVLG WGSTYGPITA AVRRLRTAGE SIAQAHLRHL NPFPRNLGAV LRRYDKVVIP
     EMNLGQLATL IRAKYLVDAH SYNQVNGMPF KAEQLATALK EAIDG
//