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Database: UniProt/SWISS-PROT
Entry: OGDHL_PONAB
LinkDB: OGDHL_PONAB
Original site: OGDHL_PONAB 
ID   OGDHL_PONAB             Reviewed;        1010 AA.
AC   Q5R9L8; Q5R854;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   20-JUN-2018, entry version 67.
DE   RecName: Full=2-oxoglutarate dehydrogenase-like, mitochondrial;
DE            EC=1.2.4.-;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1-like;
DE            Short=OGDC-E1-like;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase-like;
DE   Flags: Precursor;
GN   Name=OGDHL;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5R9L8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5R9L8-2; Sequence=VSP_029368;
CC         Note=No experimental confirmation available.;
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH91542.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CR859369; CAH91542.1; ALT_INIT; mRNA.
DR   EMBL; CR859900; CAH92056.1; -; mRNA.
DR   RefSeq; NP_001126195.1; NM_001132723.1.
DR   RefSeq; NP_001128819.1; NM_001135347.1.
DR   UniGene; Pab.18882; -.
DR   ProteinModelPortal; Q5R9L8; -.
DR   SMR; Q5R9L8; -.
DR   PRIDE; Q5R9L8; -.
DR   GeneID; 100173162; -.
DR   GeneID; 100189729; -.
DR   KEGG; pon:100173162; -.
DR   CTD; 55753; -.
DR   HOVERGEN; HBG001892; -.
DR   InParanoid; Q5R9L8; -.
DR   KO; K00164; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Complete proteome; Glycolysis;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     73       Mitochondrion. {ECO:0000255}.
FT   CHAIN        74   1010       2-oxoglutarate dehydrogenase-like,
FT                                mitochondrial.
FT                                /FTId=PRO_0000310984.
FT   CA_BIND     141    145       {ECO:0000250}.
FT   COMPBIAS     45     48       Poly-Gly.
FT   METAL       141    141       Calcium. {ECO:0000250}.
FT   VAR_SEQ     862    862       V -> VSGP (in isoform 2).
FT                                {ECO:0000303|Ref.1}.
FT                                /FTId=VSP_029368.
FT   CONFLICT     40     40       L -> F (in Ref. 1; CAH92056).
FT                                {ECO:0000305}.
FT   CONFLICT     59     59       W -> R (in Ref. 1; CAH92056).
FT                                {ECO:0000305}.
FT   CONFLICT    633    633       I -> T (in Ref. 1; CAH92056).
FT                                {ECO:0000305}.
FT   CONFLICT    657    657       R -> H (in Ref. 1; CAH92056).
FT                                {ECO:0000305}.
FT   CONFLICT    856    856       F -> S (in Ref. 1; CAH92056).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1010 AA;  114621 MW;  1E4320855FEFDA43 CRC64;
     MSQLRLLPSR LGAQAARLLA AHDIPVFGWR SRSSRPPATL PSSKGGGGSS YMEEMYFAWL
     ENPRSVHKSW DSFFRKASEE AFSGSAQPRP PSVVHESRSA VSSRTKTSKL VEDHLAVQSL
     IRAYQIRGHH VAQLDPLGIL DADLDSFVPS DLITTIDKLA FYDLQEADLD KEFQLPTTTF
     IGGSENTLSL REIIRRLENT YCQHIGLEFM FINDVEQCQW IRQKFETPGV MQFSSEEKRT
     LLARLVRSMR FEDFLARKWS SEKRFGLEGC EVMIPALKTI IDKSSEMGIE NVILGMPHRG
     RLNVLANVIR KDLEQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRVTN RNITLSLVAN
     PSHLEAVDPV VQGKTKAEQF YRGDAQGKKV MSILVHGDAA FAGQGVVYET FHLSDLPSYT
     TNGTVHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV IYVCSVAAEW
     RNTFNKDVVV DLVCYRRRGH NEMDEPMFTQ PLMYKQIHRQ VPVLKKYADK LIAEGTVTLQ
     EFEEEIAKYD RICEEAYGRS KDKKILHIKH WLDSPWPGFF NVDGEPKSMT CPATGIPEDM
     LTHIGSVASS VPLEDFKIHT GLSRILRGRA DMIKNRTVDW ALAEYMAFGS LLKEGIRVRL
     SGQDVERGTF SHRHHVLHDQ EVDRRTCVPM NHLWPDQAPY TVCNSSLSEY GVLGFELGYA
     MASPNALVLW EAQFGDFHNT AQCIIDQFIS TGQAKWVRHN GIVLLLPHGM EGMGPEHSSA
     RPERFLQMSN DDSDAYPAFT KDFEVSQLYD CNWIVVNCST PANYFHVLRR QILLPFRKPL
     IIFTPKSLLR HPEAKFSFDQ MVSGTSFQRV IPEDGAAARA PEQVRRLIFC TGKVYYDLVK
     ERSSQGLEEK VAITRLEQIS PFPFDLIKQE AEKYPGAELA WCQEEHKNMG YYDYISPRFM
     TILRRARPIW YVGRDPAAAP ATGNRNTHLV SLKKFLDTAF NLQAFEGKTF
//
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