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
//