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Database: UniProt/TrEMBL
Entry: G0S9K2_CHATD
LinkDB: G0S9K2_CHATD
Original site: G0S9K2_CHATD 
ID   G0S9K2_CHATD            Unreviewed;       482 AA.
AC   G0S9K2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 30.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=CTHT_0046180 {ECO:0000313|EMBL:EGS20113.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS20113.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R.,
RA   Devos D.P., Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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; GL988043; EGS20113.1; -; Genomic_DNA.
DR   RefSeq; XP_006694998.1; XM_006694935.1.
DR   EnsemblFungi; EGS20113; EGS20113; CTHT_0046180.
DR   GeneID; 18258656; -.
DR   KEGG; cthr:CTHT_0046180; -.
DR   KO; K00031; -.
DR   OrthoDB; EOG092C2D51; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
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: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:UP000008066};
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:UP000008066};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       78    467       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     144    146       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     378    383       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      163    169       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       320    320       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       343    343       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     146    146       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     151    151       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     178    178       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     201    201       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     328    328       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     396    396       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        208    208       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        280    280       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   482 AA;  53676 MW;  5EBE526F5FBBDAA4 CRC64;
     MSSAASSALR ASLLRSSASS RSAAAAAAAA RPAFSNLRAS PVSVSARAAP VYVFSQHFIS
     RRTMATDAPI KKIKVKNPIV ELDGDEMTRV IWKDIKEKFI YPYLDVDLKY YDLGIEYRDQ
     TNDQVTIDAA EAIKKYSVGV KCATITPDEA RVKEFNLKQM WLSPNGTIRN ILGGTVFREP
     IVIPRIPRLV PGWKKPIIIG RHAFGDQYRA KDTVIPGPGK LKMVYVPEGG EPQEIDVFEF
     KNGGGVAQTQ YNTDESIRGF AHASFKLALD KGLPLYMSTK NTILKRYDGR FKDIFQELYD
     NEYKPLFEAK GIWYEHRLID DMVAQMIKSS GGYVMALKNY DGDVQSDVVA QGFGSLGLMT
     SVLITPDGKT FESEAAHGTV TRHYREYQKG KETSTNPIAS IFAWTRGLVQ RGKLDGTPEV
     VAFAEALEQA CIDTVDIDGI MTKDLALACG KTAREDYVTT REYMDAVDKR LRKSLQEKLQ
     KL
//
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