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Database: UniProt/TrEMBL
Entry: H6SRW4_PARPM
LinkDB: H6SRW4_PARPM
Original site: H6SRW4_PARPM 
ID   H6SRW4_PARPM            Unreviewed;       458 AA.
AC   H6SRW4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   07-JUN-2017, entry version 35.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=RSPPHO_01017 {ECO:0000313|EMBL:CCG07643.1};
OS   Pararhodospirillum photometricum DSM 122.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Pararhodospirillum.
OX   NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG07643.1, ECO:0000313|Proteomes:UP000033220};
RN   [1] {ECO:0000313|EMBL:CCG07643.1, ECO:0000313|Proteomes:UP000033220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA   Duquesne K., Sturgis J.;
RT   "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL   Submitted (FEB-2012) 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; HE663493; CCG07643.1; -; Genomic_DNA.
DR   EnsemblBacteria; CCG07643; CCG07643; RSPPHO_01017.
DR   KEGG; rpm:RSPPHO_01017; -.
DR   PATRIC; fig|1150469.3.peg.1161; -.
DR   KO; K00031; -.
DR   OrthoDB; POG091H0JP0; -.
DR   Proteomes; UP000033220; 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:UP000033220};
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:CCG07643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033220};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       62    448       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND     128    130       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     362    367       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      147    153       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       304    304       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       327    327       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING     130    130       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     135    135       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     162    162       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     185    185       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     312    312       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     380    380       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        192    192       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        264    264       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   458 AA;  50833 MW;  9E78F83B389A4D81 CRC64;
     MRRSTPPSSQ RGRPGCIVLL SAWTRGVSCP TQARGTPRRT PRPSHPFTAG LSNMSKIKVK
     TPVVELDGDE MTRIIWRFIK DKLILPYLDI DLKYYDLGIE KRDETADQIT IDAANAIKTY
     GVGVKCATIT PDEARVEEFN LAKMWKSPNG TIRNILGGTV FREPIICKNV PRLVPGWTQP
     IVIGRHAFGD QYRATDVKIP GAGTLTLRFT PDDGGPGLDL EVFKFPDSGV AMAMYNLDES
     IRGFARACFN YGLTRRWPVY LSTKNTILKA YDGRFKDLFQ EVFDAEFADA FKEAGITYEH
     RLIDDMVACA MKWSGGFVWA CKNYDGDVQS DTVAQGFGSL GLMTSVLMTP DGQTIEAEAA
     HGTVTRHYRQ HQQGKETSTN PIASIFAWTQ GLKYRGTFDD TPDVVAFANA LERVCVETVE
     AGFMTKDLAI LISPDHPWLT TTAFLDKLDE GLQKAMAG
//
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