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Database: UniProt/TrEMBL
Entry: A0A142VUF0_9SPHN
LinkDB: A0A142VUF0_9SPHN
Original site: A0A142VUF0_9SPHN 
ID   A0A142VUF0_9SPHN        Unreviewed;       404 AA.
AC   A0A142VUF0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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=AOA14_02155 {ECO:0000313|EMBL:AMU93404.1};
OS   Sphingopyxis terrae NBRC 15098.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1219058 {ECO:0000313|EMBL:AMU93404.1, ECO:0000313|Proteomes:UP000076234};
RN   [1] {ECO:0000313|Proteomes:UP000076234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=203-1 {ECO:0000313|Proteomes:UP000076234};
RA   Yoshiyuki O., Shouta N., Nagata Y., Numata M., Tsuchikane K.,
RA   Hosoyama A., Yamazoe A., Tsuda M., Fujita N., Kawai F.;
RT   "Complete genome sequence of a polyethylene glycol-degrading strain
RT   Sphingopyxis terrae strain 203-1 (NBRC 15098).";
RL   Submitted (NOV-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; CP013342; AMU93404.1; -; Genomic_DNA.
DR   RefSeq; WP_062900589.1; NZ_CP013342.1.
DR   EnsemblBacteria; AMU93404; AMU93404; AOA14_02155.
DR   KEGG; ster:AOA14_02155; -.
DR   KO; K00031; -.
DR   Proteomes; UP000076234; 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:UP000076234};
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:AMU93404.1};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN        9    394       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      75     77       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     308    313       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION       94    100       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       250    250       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       273    273       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     258    258       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     326    326       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        210    210       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   404 AA;  45369 MW;  0DBEF2A6BA9BA0E5 CRC64;
     MGKIKVVNPV VELDGDEMTR IIWQWIRERL ILPYLDVDLH YYDLGIEERD RTDDKITVEA
     ANAIKKYGVG VKCATITPDE ARVEEFGLKK MWKSPNGTIR NILGGVVFRE PIVIKNVPRL
     VPGWTDPIVV GRHAFGDQYR ATDYRVPGPG KLRLVFEGED GTIIDEEVFQ FPSSGVAMAM
     YNLDDSIRDF ARASMNYGLA RGWPVYLSTK NTILKAYDGR FKDLFEEVYQ NEFKAKFEAA
     GIIYEHRLID DMVASALKWS GKFVWACKNY DGDVQSDTVA QGFGSLGLMT SVLMTPDGQT
     VESEAAHGTV TRHYRMHQQG KATSTNPIAS IFAWTGGLKH RGKLDGTPEV TKFAEDLERV
     CIETVESGKM TKDLALLIGP DQNWLTTEGF FEAIVENLEK KMGS
//
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