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Database: UniProt/TrEMBL
Entry: W5WTC9_9PSEU
LinkDB: W5WTC9_9PSEU
Original site: W5WTC9_9PSEU 
ID   W5WTC9_9PSEU            Unreviewed;       407 AA.
AC   W5WTC9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   07-JUN-2017, entry version 18.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=KALB_8052 {ECO:0000313|EMBL:AHI01410.1};
OS   Kutzneria albida DSM 43870.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Kutzneria.
OX   NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI01410.1, ECO:0000313|Proteomes:UP000019225};
RN   [1] {ECO:0000313|EMBL:AHI01410.1, ECO:0000313|Proteomes:UP000019225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI01410.1};
RX   PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA   Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA   Bechthold A., Kalinowski J., Luzhetskyy A.;
RT   "Complete genome sequence of producer of the glycopeptide antibiotic
RT   Aculeximycin Kutzneria albida DSM 43870T, a representative of minor
RT   genus of Pseudonocardiaceae.";
RL   BMC Genomics 15:885-885(2014).
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; CP007155; AHI01410.1; -; Genomic_DNA.
DR   RefSeq; WP_025361223.1; NZ_CP007155.1.
DR   EnsemblBacteria; AHI01410; AHI01410; KALB_8052.
DR   KEGG; kal:KALB_8052; -.
DR   PATRIC; fig|1449976.3.peg.8090; -.
DR   KO; K00031; -.
DR   Proteomes; UP000019225; 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:UP000019225};
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:UP000019225};
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   407 AA;  44954 MW;  9494D11B570EFE79 CRC64;
     MGKIKVEGTV VELDGDEMTR IIWQFIKDKL IHPYLDVNLD YYDLGIEHRD ATDDQVTIDS
     ANAIKRHGVG VKCATITPDE ARVEEFGLKK MWVSPNGTIR NILGGVVFRE PIIISNIPRL
     VPGWTKPIII GRHAHGDQYK ATNFKVPGPG ELTITFTPAD GSEPIQHVVA NYPEGGGVAM
     GMFNFRKSIE DFARASFSYG LQRNYPVYMS TKNTILKAYD GMFKDVFQEI FDAEFKAEFD
     SKGLTYEHRL IDDMVAAAMK WEGGYVWACK NYDGDVQSDT VAQGFGSLGL MTSVLMTPDG
     KTVEAEAAHG TVTRHYRQHQ QGKPTSTNPI ASIYAWTGGL KHRGKLDGTP AVTGFAEALE
     QVVISTVESG SMTKDLALLV GPDQAWQTTE DFLGTLDENL QKRMASS
//
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