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Database: UniProt/TrEMBL
Entry: A0A0C5BRD4_9MICO
LinkDB: A0A0C5BRD4_9MICO
Original site: A0A0C5BRD4_9MICO 
ID   A0A0C5BRD4_9MICO        Unreviewed;       405 AA.
AC   A0A0C5BRD4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   07-JUN-2017, entry version 17.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   ORFNames=VT73_04130 {ECO:0000313|EMBL:KKM46243.1};
OS   Rathayibacter toxicus.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM46243.1, ECO:0000313|Proteomes:UP000052979};
RN   [1] {ECO:0000313|EMBL:KKM46243.1, ECO:0000313|Proteomes:UP000052979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FH142 {ECO:0000313|EMBL:KKM46243.1,
RC   ECO:0000313|Proteomes:UP000052979};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.;
RT   "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA
RT   70134 or CS 32), a Western Australian isolate.";
RL   Submitted (APR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKM46243.1}.
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DR   EMBL; LBFI01000024; KKM46243.1; -; Genomic_DNA.
DR   RefSeq; WP_027692515.1; NZ_LBFI01000024.1.
DR   EnsemblBacteria; KKM46243; KKM46243; VT73_04130.
DR   KEGG; rtc:APU90_03365; -.
DR   KEGG; rtx:TI83_03105; -.
DR   PATRIC; fig|145458.7.peg.731; -.
DR   KO; K00031; -.
DR   Proteomes; UP000052979; Unassembled WGS sequence.
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:UP000052979};
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:KKM46243.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052979};
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       251    251       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       274    274       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     259    259       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        211    211       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   405 AA;  45329 MW;  C429654C8B81A2CE CRC64;
     MSTIKVKGTV VELDGDEMTR IIWQKIKDTL IHPYLEVNLD YYDLGIENRD RTDDQVTIDA
     AHAIQKHGVG VKCATITPDE ARVEEFGLKK MWKSPNGTIR NILGGVIFRE PIIISNIPRL
     VPGWNKPIII GRHAFGDQYR ATDFVFKGAG TLTVEFTPDD GSEPMKLEVY HAPDDGIAQV
     QYNQDASIRD FARASLTYGL ARNYPVYLST KNTILKAYDG RFKDIFEEIF ETEFRDRFAA
     AGLTYEHRLI DDMVASAMKW EGGYVWACKN YDGDVQSDTV AQGFGSLGLM TSVLSTPDGR
     VVEAEAAHGT VTRHYRQHQQ GKPTSTNPIA SIYAWTRGLT HRGTLDGNQE LIDFALTLED
     VVVKTVESGK MTKDLALLVG PDQPWQTTEE FLAALDENLR VRMSA
//
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