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Database: UniProt/TrEMBL
Entry: A0A0D4C2E0_9MICC
LinkDB: A0A0D4C2E0_9MICC
Original site: A0A0D4C2E0_9MICC 
ID   A0A0D4C2E0_9MICC        Unreviewed;       409 AA.
AC   A0A0D4C2E0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   07-JUN-2017, entry version 13.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=UM93_16755 {ECO:0000313|EMBL:AJT42709.1};
OS   Arthrobacter sp. IHBB 11108.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT42709.1, ECO:0000313|Proteomes:UP000061839};
RN   [1] {ECO:0000313|EMBL:AJT42709.1, ECO:0000313|Proteomes:UP000061839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT42709.1,
RC   ECO:0000313|Proteomes:UP000061839};
RX   PubMed=25908143;
RA   Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter
RT   sp. Strain IHBB 11108 Using PacBio Single-Molecule Real-Time
RT   Sequencing Technology.";
RL   Genome Announc. 3:0-0(2015).
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; CP011005; AJT42709.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJT42709; AJT42709; UM93_16755.
DR   KEGG; ari:UM93_16755; -.
DR   PATRIC; fig|1618207.4.peg.3404; -.
DR   KO; K00031; -.
DR   Proteomes; UP000061839; 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:UP000061839};
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   ECO:0000313|EMBL:AJT42709.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061839};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       12    399       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      78     80       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     313    318       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION       97    103       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      80     80       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING      85     85       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     112    112       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     135    135       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        142    142       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        215    215       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   409 AA;  45527 MW;  7477448E0C7265CD CRC64;
     MAEAAKIKVV GPVVELDGDE MTRIIWQFIK DRLIHPYLDI DLRYYDLSIQ NRDATDDQVT
     VDAANAIKEH HVGVKCATIT PDEARVEEFG LKKMWVSPNG TIRNILGGVV FREPIIISNI
     PRLVPGWNKP IIIGRHAFGD QYRATNFKVP GPGTLTLTFT PADGGEEIKQ QVVTYPEEGG
     VAMGMYNFNE SIKDFARASF AYGLQRNYPV YLSTKNTILK AYDGQFKDLF QEVFDNEFKE
     QFDAAGLTYE HRLIDDMVAS AMKWEGGYVW ACKNYDGDVQ SDTVAQGFGS LGLMTSVLMT
     PDGKTVEAEA AHGTVTRHYR QHQQGKPTST NPIASIFAWT RGLMHRGKID NTPEVVQFAE
     TLEDVVIKTV ESGKMTKDLA LLVSPDQAFL TTEDFLAALD ENLSARLAG
//
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