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Database: UniProt/TrEMBL
Entry: A7TGF1_VANPO
LinkDB: A7TGF1_VANPO
Original site: A7TGF1_VANPO 
ID   A7TGF1_VANPO            Unreviewed;       427 AA.
AC   A7TGF1;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=Kpol_1055p78 {ECO:0000313|EMBL:EDO18721.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294)
OS   (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO18721.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
RA   Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two
RT   yeast species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2)
CC       + NADPH. {ECO:0000256|PIRNR:PIRNR000108}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC         ECO:0000256|PIRSR:PIRSR000108-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3};
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|PIRNR:PIRNR000108}.
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DR   EMBL; DS480386; EDO18721.1; -; Genomic_DNA.
DR   RefSeq; XP_001646579.1; XM_001646529.1.
DR   ProteinModelPortal; A7TGF1; -.
DR   STRING; 436907.XP_001646579.1; -.
DR   EnsemblFungi; EDO18721; EDO18721; Kpol_1055p78.
DR   GeneID; 5547031; -.
DR   KEGG; vpo:Kpol_1055p78; -.
DR   eggNOG; KOG1526; Eukaryota.
DR   eggNOG; COG0538; LUCA.
DR   InParanoid; A7TGF1; -.
DR   KO; K00031; -.
DR   OrthoDB; EOG092C2D51; -.
DR   PhylomeDB; A7TGF1; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:EnsemblFungi.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR004790; Isocitrate_DH_NADP.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11822; PTHR11822; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000267};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000108,
KW   ECO:0000256|PIRSR:PIRSR000108-3};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000108,
KW   ECO:0000256|PIRSR:PIRSR000108-3};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000108,
KW   ECO:0000256|PIRSR:PIRSR000108-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-4};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000108};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       20    410       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      86     88       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     321    326       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      105    111       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       263    263       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       286    286       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING      88     88       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING      93     93       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     120    120       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     143    143       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     271    271       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     339    339       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        150    150       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        223    223       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   427 AA;  47765 MW;  ECF719C5D2C33269 CRC64;
     MSRAYSSAAR KLSKITVKSP LVELDGDEMT RIIWSKIKKN LILPFLDVDL KYYDLSIENR
     DSTNDQVTVD AANAIKNFGV GVKCATITPD EARVEEFNLK KMWKSPNGTI RNILGGTVFR
     EPIVIPRIPR LIPGWEKPII IGRHAHGDQY KATDTLIPTA GKLELVFTPT DPNGERQILN
     VYDYKNSGVA LAMYNTDESI RGFAHSSFKL AINKKLNLFL STKNTILKKY DGRFKDIFQE
     IYESDYKSQF ENLGISYEHR LIDDMVAQMI KSKGGFIMAL KNYDGDVQSD IVAQGFGSLG
     LMTSVLVTPD GKTFESEAAH GTVTRHYRQY EQGKETSTNS IASIFAWSRG LAKRGELDST
     PDVIKFANLL ESATLNTVQQ DGIMTKDLAL ACGKTERSAY VTTDEFLDAV ATRLNNEFKS
     FENSSKL
//
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