ID A0A081XMV2_STRTO Unreviewed; 1175 AA.
AC A0A081XMV2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=2-oxoacid ferredoxin oxidoreductase {ECO:0000313|EMBL:KES04875.1};
GN ORFNames=BU52_22800 {ECO:0000313|EMBL:KES04875.1};
OS Streptomyces toyocaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=55952 {ECO:0000313|EMBL:KES04875.1, ECO:0000313|Proteomes:UP000028341};
RN [1] {ECO:0000313|EMBL:KES04875.1, ECO:0000313|Proteomes:UP000028341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15009 {ECO:0000313|EMBL:KES04875.1,
RC ECO:0000313|Proteomes:UP000028341};
RA Hong H.-J., Kwun M.J.;
RT "The genome announcement of Streptomyces toyocaensis NRRL15009.";
RL Submitted (FEB-2014) 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:KES04875.1}.
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DR EMBL; JFCB01000022; KES04875.1; -; Genomic_DNA.
DR RefSeq; WP_051858493.1; NZ_JFCB01000022.1.
DR AlphaFoldDB; A0A081XMV2; -.
DR STRING; 55952.BU52_22800; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000028341; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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 GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR046667; DUF6537.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028341};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 456..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT DOMAIN 731..917
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 961..1155
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1175 AA; 125518 MW; 31A37105EEF590F1 CRC64;
MTSSFTEAGR QDGRHLRLDD RYRLPDGVVH LSGIQALVRI LLDRSARDRR DGLRTATFVS
GYEGSPLAGY DIELARRQAL LREYDVVHKP GLNEELAATS VMGSQLAGQV GMSRYDGVMG
IWYGKSPGLD RASDALRHAN LVGTARLGGA VALVGNDPGA KSSSVPCVSE ATLADLAIPT
LYPADSQDVL DFGIHAQYLS RFSGLWAGMK ITTAVADAMS TAVVTPNRIA VVEGDAGPSP
HRPSAMLLGP ELMALERSLH DSRLPRALEY ARLHGLNRVV QRGPSDRIGI LASGKTYLDV
REALRVIGLT DADLTRQGIR ILKLGMVFPL ERDAVVEFAE GLDHLLVVEE KRPFLEAAVK
EILYGRAQVP TVHGKEGPDG QPLFSRSGEL DTDGVTSGLS RVLAALGVEA ARVWRRRPGP
RATLSLPLLA RSPYYCSGCP HNTSTTAGGD SPVGAGIGCH AMVVFMDAEQ VGTVVGMTQM
GGEGAQWIGM QPFVDVGHFV QNIGDGTFMH SGSLAVRAAV AAGVNVTFKL LYNGTVAMTG
GQDAVGALPV DRLAATLLDE GVAKVIITTD NKARVPRARL PRAVRVLDRA GIEKALAELR
ATAGVTVLIH DQECAAEKRR ARRRGKAGTP TTRVWINERL CEGCGDCGRA SNCLSVHPVP
TEFGRKTRID QSSCNLDYSC LDGDCPAFMT ITPAGRPRHA GPPALAAGDV PEPAVRRTSD
GSFGMRITGI GGTGIVTVSQ VLATAAVIDG QHARSLDQTG LAQKGGAVVS DIKITAQAVE
QGAKLTERSC DLYLACDPLV ATDPTYLRVA SPERTVAVMS TTEIPTGQMV VDTEVGFPAP
DVVRHAVGEV SRQLVALDTG ALATQLFDDE QYANMLLVGA AYQTGVLPVP ARAVEEAITL
NGVAVECNIQ AFRRGRQAIA DPEALRAAVA GPAPEEIAGP PLPRGTTELV ATVTGDEGSE
LHRLLTVRVA DLIGYQDLRY ARRYAEFVRR VADAERAAVD GSTELTEAAA RYLHKLMAYK
DEYEVARLAL DPVVDADIDA AFGSGSRRSS LLRPPVLRAV GMERKIAVGR WARPVLVLLR
ALRRVRGTRL DLFGLHPVRR VERELAEDYR ASLGASLALL TEETLPVVRR LAELPDVVRG
YEGVKLASVE RYRAEKDSIL AALREGAEHV TTEAG
//
