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Database: UniProt/TrEMBL
Entry: A0A191WDH2_9MICO
LinkDB: A0A191WDH2_9MICO
Original site: A0A191WDH2_9MICO 
ID   A0A191WDH2_9MICO        Unreviewed;       405 AA.
AC   A0A191WDH2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   07-JUN-2017, entry version 7.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=ATC03_05910 {ECO:0000313|EMBL:ANJ26320.1};
OS   Agromyces aureus.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agromyces.
OX   NCBI_TaxID=453304 {ECO:0000313|EMBL:ANJ26320.1, ECO:0000313|Proteomes:UP000078437};
RN   [1] {ECO:0000313|Proteomes:UP000078437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR33 {ECO:0000313|Proteomes:UP000078437};
RA   Corretto E., Antonielli L., Sessitsch A., Brader G.;
RT   "Complete genome sequence of Agromyces aureus AR33T and comparison
RT   with related organisms.";
RL   Submitted (JAN-2016) 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; CP013979; ANJ26320.1; -; Genomic_DNA.
DR   RefSeq; WP_067874308.1; NZ_CP013979.1.
DR   EnsemblBacteria; ANJ26320; ANJ26320; ATC03_05910.
DR   KEGG; agy:ATC03_05910; -.
DR   KO; K00031; -.
DR   Proteomes; UP000078437; 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:UP000078437};
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    395       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      75     77       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     309    314       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION       94    100       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       251    251       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       274    274       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     259    259       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     327    327       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        211    211       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   405 AA;  45162 MW;  86F1BDFAAD88010E CRC64;
     MSKIKVEGTV VELDGDEMTR IIWQAIKDQL IHPYLDVNLE YYDLSIQKRD ETDDQITVDA
     AHAIQKHGVG VKCATITPDE ARVEEFGLKK MWRSPNGTIR NILGGVIFRE PIIISNIPRL
     VPGWNKPIIV GRHAFGDQYR ATDFRFEGEG TLTMTFTPKD GSEPQQFEVF QSPGSGVAMG
     MYNLDESIRD FARASLNYGL SRNYPVYLST KNTILKAYDG RFKDLFQEVF EAEFKEAFDA
     AGLTYEHRLI DDMVAASLKW EGGYVWACKN YDGDVQSDTV AQGFGSLGLM TSVLATPDGR
     VVEAEAAHGT VTRHYRQHQQ GKPTSTNPIA SIYAWTRGLA HRGKLDGNQE LIDFSLTLED
     VVIKTVESGA MTKDLAALVG PEQAYQTTEE FLQTLSDNLK ARIAA
//
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