GenomeNet

Database: UniProt/TrEMBL
Entry: S7RBY2_GLOTA
LinkDB: S7RBY2_GLOTA
Original site: S7RBY2_GLOTA 
ID   S7RBY2_GLOTA            Unreviewed;       419 AA.
AC   S7RBY2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   07-JUN-2017, entry version 21.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=GLOTRDRAFT_132578 {ECO:0000313|EMBL:EPQ51760.1};
OS   Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617)
OS   (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX   NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ51760.1, ECO:0000313|Proteomes:UP000030669};
RN   [1] {ECO:0000313|EMBL:EPQ51760.1, ECO:0000313|Proteomes:UP000030669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ51760.1,
RC   ECO:0000313|Proteomes:UP000030669};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A.,
RA   Henrissat B., Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S.,
RA   Aerts A., Benoit I., Boyd A., Carlson A., Copeland A., Coutinho P.M.,
RA   de Vries R.P., Ferreira P., Findley K., Foster B., Gaskell J.,
RA   Glotzer D., Gorecki P., Heitman J., Hesse C., Hori C., Igarashi K.,
RA   Jurgens J.A., Kallen N., Kersten P., Kohler A., Kuees U.,
RA   Kumar T.K.A., Kuo A., LaButti K., Larrondo L.F., Lindquist E.,
RA   Ling A., Lombard V., Lucas S., Lundell T., Martin R., McLaughlin D.J.,
RA   Morgenstern I., Morin E., Murat C., Nagy L.G., Nolan M., Ohm R.A.,
RA   Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J., Sabat G., Salamov A.,
RA   Samejima M., Schmutz J., Slot J.C., St John F., Stenlid J., Sun H.,
RA   Sun S., Syed K., Tsang A., Wiebenga A., Young D., Pisabarro A.,
RA   Eastwood D.C., Martin F., Cullen D., Grigoriev I.V., Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed
RT   from 31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; KB469309; EPQ51760.1; -; Genomic_DNA.
DR   RefSeq; XP_007869663.1; XM_007871472.1.
DR   EnsemblFungi; EPQ51760; EPQ51760; GLOTRDRAFT_132578.
DR   GeneID; 19302529; -.
DR   KEGG; gtr:GLOTRDRAFT_132578; -.
DR   KO; K00031; -.
DR   Proteomes; UP000030669; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; 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: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:UP000030669};
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:UP000030669};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       13    404       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      79     81       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     313    318       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION       98    104       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       255    255       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       278    278       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING      81     81       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING      86     86       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     113    113       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     136    136       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     263    263       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     331    331       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        143    143       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        215    215       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   419 AA;  47169 MW;  72AC5DD6B97D1515 CRC64;
     MARLQQKIAV KNPVVELDGD EMTRIIWKKI REELILPYLE LDIKYYDLGL EYRDATNDQV
     TVDAANAILE HKVGIKCATI TPDEARVKEF NLKQMWKSPN GTIRNILGGT VFREPIILEK
     IPKPVPGWVK PIVIGRHAFG DQYRATDFIA PGPGKLQLVF TPDNGGEKTT LDVYDFKGKG
     VALSMYNTDD SISGFAHSSF KMALSKKMTL FMSTKNTILK KYDGRFKDIF QEIYDTQYKS
     EFEKLGIYYE HRLIDDMVAQ AIKSSGGFVW ACKNYDGDVQ SDILAQGFGS LGMMTSELIT
     PDGDVVESEA AHGTVTRHYR EYQKGNETST NPVASIFAWT RGLIHRAKLD GNDALRQFCQ
     DLEAACVEVI DQEGIMTKDL ALAIHGKNMK REHWVLTNEY MDAVGKRLNS KLASRGAKL
//
DBGET integrated database retrieval system