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Database: UniProt
Entry: A0A498KTG5_MALDO
LinkDB: A0A498KTG5_MALDO
Original site: A0A498KTG5_MALDO 
ID   A0A498KTG5_MALDO        Unreviewed;      1251 AA.
AC   A0A498KTG5;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00040267};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1 {ECO:0000256|ARBA:ARBA00042984};
GN   ORFNames=DVH24_023136 {ECO:0000313|EMBL:RXI08992.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI08992.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXI08992.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXI08992.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-oxoglutarate
CC       dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and
CC       lipoamide dehydrogenase (E3). {ECO:0000256|ARBA:ARBA00037426}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006936}.
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:RXI08992.1}.
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DR   EMBL; RDQH01000327; RXI08992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498KTG5; -.
DR   STRING; 3750.A0A498KTG5; -.
DR   Proteomes; UP000290289; Chromosome 1.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd01867; Rab8_Rab10_Rab13_like; 1.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOGLUTARATE DEHYDROGENASE E1 COMPONENT DHKTD1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS51419; RAB; 1.
DR   PROSITE; PS51421; RAS; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          866..1079
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   1251 AA;  140760 MW;  E1EADC7782A489BE CRC64;
     MATAQPARGR TDYDYLIKLL LIGDSGVGKS CLLLRFSDGS FTTSFITTIG IDFKIRTIEL
     DGKRIKLQIW DTAGQERFRT ITTAYYRGAM GILLVYDVTD ESSFNNIRNW IRNIEQHASV
     NVNKILVGNK ADMDESRRAV PTSRGQALAD EYGIKFFETS AKTNLNVEEV FFSIARDIKQ
     RLAESDARGT EPQTLRINED RAGGQAAQNS SCCVSNAAAA LSEQQSSIGL VAMSWFRAGS
     GVAKLAIRRS LSNSGSYAAR RRVLPSQSRD FHTTIPKSKA APVPHPVPLS RLTDSFLDGT
     SSVYLEGLQR AWEADPNSVD ESWDNFFRNF VGQASTSPGI SGQTIQESMR LLLLVRAYQV
     NGHMKAKLDP LGLEEREIPD DLDPALYGFT EADLDREFFL GVWRMAGFLS ENRPVQTLRS
     ILTRLEQAYC GTIGYEYMHI ADRERCNWLR NKIETPTPMQ YNRQRREVIL DRLIWSTQFE
     NFLATKWTAA KRFGLEGGET LIPGMKEMFD RSADLGVESI VIGMSHRGRL NVLGNVVRKP
     LRHIFSEFSG GTKPVDEDGL YTGTGDVKYH LGTSYDRPTR GGKRIHLSLV ANPSHLEAVD
     PVVVGKTRAK QYYSNDADRT KNMGVLIHGD GSFAGQGVVY ETLHLSALPN YTTGGTIHIV
     VNNQVAFTTD PMSGRSSQYC TDVAKALNAP IFHVNADDVE AVVHVCELAA EWRQTFHSDV
     VVDLVCYRRF GHNEIDEPSF TQPKMYKVIR NHPSALTIYQ NKLLESGQVA KEDIERIQSK
     VNEILNEEFL ASKDYTLQRR DWLSSHWSGF KSPEQISRIR NTGVKPEILK SVGKAVTALP
     ETLKPHRAVK KVYEQRAQMI ATGEGIDWAV AEALAFATLL VEGNHVRLSG QDVERGTFSH
     RHSVIHDQET GEKYCPLDHI TAGQDEEMFT VSNSSLSEFG VLGFELGYSM ESPNALVIWE
     AQFGDFANGA QVIFDQFLSS GESKWLRQTG LVVLLPHGYD GQGPEHSSAR LERFLQMSDD
     HPFVIPEMDP TLRKQIQECN WQVVNVTTPA NYFHVLRRQL HREFRKPLIV MAPKNLLRHK
     DCKSNLSEFD DVQGHPGFDK QGTRFKRLIK DQNGHSDLEE GIRRLVLCSG KVYYELDEER
     RKVEAKDVAI CRVEQLCPFP YDLIQRELKR YPNAEIVWVQ EEPMNMGAYS YIAPRLSTAM
     KSLGRGTFDD IKYIGRAPSA ATATGFYTVH LKEQSEIVHK AVQKEPIEFP S
//
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