(data stored in SCRATCH zone)

SWISSPROT: B6HGF9_PENRW

ID   B6HGF9_PENRW            Unreviewed;       486 AA.
AC   B6HGF9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=Pc20g03610 {ECO:0000313|EMBL:CAP85690.1}, PCH_Pc20g03610
GN   {ECO:0000313|EMBL:CAP85690.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85690.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85690.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920435; CAP85690.1; -; Genomic_DNA.
DR   RefSeq; XP_002562912.1; XM_002562866.1.
DR   STRING; 500485.XP_002562912.1; -.
DR   EnsemblFungi; CAP85690; CAP85690; PCH_Pc20g03610.
DR   GeneID; 8309966; -.
DR   KEGG; pcs:Pc20g03610; -.
DR   eggNOG; KOG1526; Eukaryota.
DR   eggNOG; COG0538; LUCA.
DR   HOGENOM; HOG000019858; -.
DR   KO; K00031; -.
DR   OMA; AMGMYNQ; -.
DR   OrthoDB; EOG092C2D51; -.
DR   BioCyc; PCHR:PC20G03610-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
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;
DR   PRODOM; B6HGF9.
DR   SWISS-2DPAGE; B6HGF9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
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:UP000000724};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       86    474       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     152    154       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     385    390       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      171    177       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       327    327       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       350    350       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     154    154       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     159    159       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     186    186       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     209    209       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     335    335       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     403    403       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        216    216       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        287    287       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   486 AA;  54181 MW;  03F0FDE9E2748391 CRC64;
     MNALRSSSAV ARRSLATPPA PLSSTSRLIS SSSFTSSLSK RSISSTSLSQ RTNRVAASSR
     WSGSIPSSIT QIRTMASETK IKVKNPVVEL DGDEMTRIIW QEIREKLILP YLDIDLKYYD
     LGIEYRDETN DQVTIDAAEA IKKYGVGVKC ATITPDEARV EEFKLKKMWL SPNGTIRNIL
     GGTVFREPIV IPRIPRLVPG WTKPIIIGRH AFGDQYRAQD RVIPGPGKLE LVYTPAGGEP
     ERVQVFDFQG GGVTQCQYNT DESIAGFAHS SFKMALMKGL PLYMSTKNTI LKKYDGRFKD
     IFEEIFQKDY KKDFDAKNIW YEHRLIDDMV AQMIKSEGGF VMALKNYDGD VQSDIVAQGF
     GSLGLMTSAL ATPDGSAYES EAAHGTVTRH YREHQKGNET STNPIASIFA WTRGLVQRGQ
     LDNTPEVVTF AEELERACVD VVNDEAIMTK DLALACGRKD RESWVTTGEY MAAVERRLKA
     NLKARL
//

If you have problems or comments...

PBIL Back to PBIL home page