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Database: UniProt/TrEMBL
Entry: A0A1W6DT94_9MICO
LinkDB: A0A1W6DT94_9MICO
Original site: A0A1W6DT94_9MICO 
ID   A0A1W6DT94_9MICO        Unreviewed;       405 AA.
AC   A0A1W6DT94;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   22-NOV-2017, entry version 4.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=B8281_17120 {ECO:0000313|EMBL:ARK06192.1};
OS   Cellulosimicrobium sp. TH-20.
OC   Bacteria; Actinobacteria; Micrococcales; Promicromonosporaceae;
OC   Cellulosimicrobium.
OX   NCBI_TaxID=1980001 {ECO:0000313|EMBL:ARK06192.1, ECO:0000313|Proteomes:UP000193765};
RN   [1] {ECO:0000313|EMBL:ARK06192.1, ECO:0000313|Proteomes:UP000193765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH-20 {ECO:0000313|EMBL:ARK06192.1,
RC   ECO:0000313|Proteomes:UP000193765};
RA   Zheng F.;
RT   "Genome Sequencing of Strain Cellulosimicrobium sp. TH-20 with Ginseng
RT   Biotransformation Ability.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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; CP020857; ARK06192.1; -; Genomic_DNA.
DR   KEGG; cet:B8281_17120; -.
DR   KO; K00031; -.
DR   Proteomes; UP000193765; Chromosome.
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:UP000193765};
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   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN        9    396       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      75     77       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     310    315       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION       94    100       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       252    252       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       275    275       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING      77     77       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING      82     82       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     109    109       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     132    132       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     260    260       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     328    328       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        139    139       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        212    212       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   405 AA;  45173 MW;  2CCBAF88835556AC CRC64;
     MGKIKVVNPV VELDGDEMTR IIWQFIKDRL IHPYLDVDLK YYDLSIQNRD ATDDQVTIDA
     AHAIKQYNVG VKCATITPDE ARVEEFGLKK MWVSPNGTIR NILGGVVFRE PIIISNIPRL
     VPGWNKPIII GRHAHGDQYK STNFKVPGPG KITMTFEPAD GSEAQKFEVV TMPEEGGVAM
     GMYNFNESIR DFARASFAYG LQREYPVYLS TKNTILKAYD GAFKDIFQEV FDAEFAEAFA
     AKGITYEHRL IDDMVASAMK WEGGYVWACK NYDGDVQSDT VAQGFGSLGL MTSVLMTPDG
     QTVEAEAAHG TVTRHYRQHQ QGKPTSTNPI ASIFAWTRGL MHRGKLDGTP EVTEFAQTLE
     DVVIKTVESG KMTKDLALLI GPDQEWLTTE EFLAALDENL KARLG
//
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