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Database: UniProt/TrEMBL
Entry: A0A0N9IBD0_9PSEU
LinkDB: A0A0N9IBD0_9PSEU
Original site: A0A0N9IBD0_9PSEU 
ID   A0A0N9IBD0_9PSEU        Unreviewed;       404 AA.
AC   A0A0N9IBD0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=AOZ06_48900 {ECO:0000313|EMBL:ALG13740.1};
OS   Kibdelosporangium phytohabitans.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Kibdelosporangium.
OX   NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG13740.1, ECO:0000313|Proteomes:UP000063699};
RN   [1] {ECO:0000313|EMBL:ALG13740.1, ECO:0000313|Proteomes:UP000063699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG13740.1,
RC   ECO:0000313|Proteomes:UP000063699};
RA   Qin S., Xing K.;
RT   "Genome sequencing of Kibdelosporangium phytohabitans.";
RL   Submitted (JUL-2015) 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; CP012752; ALG13740.1; -; Genomic_DNA.
DR   RefSeq; WP_054295626.1; NZ_CP012752.1.
DR   EnsemblBacteria; ALG13740; ALG13740; AOZ06_48900.
DR   KEGG; kphy:AOZ06_48900; -.
DR   KO; K00031; -.
DR   Proteomes; UP000063699; 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:UP000063699};
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:ALG13740.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063699};
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       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     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        212    212       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   404 AA;  44810 MW;  6717F8B718D76F90 CRC64;
     MAKIKVQGTV VELDGDEMTR IIWQFIKDKL IHPYLDINLD YYDLGIEHRD ATDDQVTVDA
     ANAISRHGVG VKCATITPDE ARVEEFGLKK MWLSPNGTIR NILGGVIFRE PIVISNIPRL
     VPGWTKPIII GRHAHGDQYK AQNFKVPGAG ELTITFTPED GSEPIQHVIA NYGPDGGVAL
     GMFNFNKSIE DFARASLRYG LEREYPVYMS TKNTILKAYD GAFKDIFQRV YEEEFKADFD
     AKGLTYEHRL IDDMVAAALK WEGGYVWACK NYDGDVQSDT VAQGFGSLGL MTSVLMTPDG
     KVEAEAAHGT VTRHYRQHQA GKPTSTNPIA SIYAWTRGLD ARAKQDSTPE VAGFANALEQ
     VVVETVESGK MTKDLALLVG PDQAWQTTEE FLATLDENLQ KKMA
//
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