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Database: UniProt/TrEMBL
Entry: A7IP44_XANP2
LinkDB: A7IP44_XANP2
Original site: A7IP44_XANP2 
ID   A7IP44_XANP2            Unreviewed;       404 AA.
AC   A7IP44;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   07-JUN-2017, entry version 71.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   OrderedLocusNames=Xaut_4569 {ECO:0000313|EMBL:ABS69790.1};
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245 {ECO:0000313|EMBL:ABS69790.1, ECO:0000313|Proteomes:UP000002417};
RN   [1] {ECO:0000313|EMBL:ABS69790.1, ECO:0000313|Proteomes:UP000002417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2 {ECO:0000313|Proteomes:UP000002417};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.,
RA   Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Brainard J.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ensigns S.A., Richardson P.;
RT   "Complete sequence of chromosome of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) 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; CP000781; ABS69790.1; -; Genomic_DNA.
DR   RefSeq; WP_012116540.1; NC_009720.1.
DR   ProteinModelPortal; A7IP44; -.
DR   STRING; 78245.Xaut_4569; -.
DR   EnsemblBacteria; ABS69790; ABS69790; Xaut_4569.
DR   KEGG; xau:Xaut_4569; -.
DR   eggNOG; ENOG4105D5N; Bacteria.
DR   eggNOG; COG0538; LUCA.
DR   HOGENOM; HOG000019858; -.
DR   KO; K00031; -.
DR   OMA; AMGMYNQ; -.
DR   OrthoDB; POG091H0JP0; -.
DR   BioCyc; XAUT78245:GHS6-4589-MONOMER; -.
DR   Proteomes; UP000002417; 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:UP000002417};
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:ABS69790.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002417};
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;  45112 MW;  D485D188AEC0EA06 CRC64;
     MAKIKVANPV VELDGDEMTR IIWQYIKDKL IHPYLDIDLE YYDLSVENRD ATSDKVTVDA
     ANAIKKHGVG VKCATITPDE ARVEEFKLKE MWKSPNGTIR NILGGVIFRE PIICKNVPRL
     VPGWTQPIVV GRHAFGDQYR ATDFKVPGKG TLTVTFVGED GTKIEKEVYK FPGAGVALSM
     YNLDESIREF ARASLNYGLI RNYPVYLSTK NTILKAYDGR FKDIFQEVYE AEFKAEFDKR
     GLTYEHRLID DMVASALKWS GGYVWACKNY DGDVQSDIVA QGFGSLGLMT SVLMTPDGQT
     VEAEAAHGTV TRHYREHQKG KETSTNSIAS IFAWTRGLSH RAKLDGNDEL AKFAATLEKV
     CVDTVEEGYM TKDLALLVGA DQKWLSTTGF LDKISENLTK AMAA
//
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