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Database: UniProt/TrEMBL
Entry: A5CU33_CLAM3
LinkDB: A5CU33_CLAM3
Original site: A5CU33_CLAM3 
ID   A5CU33_CLAM3            Unreviewed;       404 AA.
AC   A5CU33;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   07-JUN-2017, entry version 74.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   Name=icdA {ECO:0000313|EMBL:CAN02619.1};
GN   OrderedLocusNames=CMM_2537 {ECO:0000313|EMBL:CAN02619.1};
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Clavibacter.
OX   NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN02619.1, ECO:0000313|Proteomes:UP000001564};
RN   [1] {ECO:0000313|EMBL:CAN02619.1, ECO:0000313|Proteomes:UP000001564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN02619.1,
RC   ECO:0000313|Proteomes:UP000001564};
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA   Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O.,
RA   Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S.,
RA   Ruckert C., Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R.,
RA   Kaiser O., Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island
RT   involved in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN02619.1; -; Genomic_DNA.
DR   RefSeq; WP_012039226.1; NC_009480.1.
DR   ProteinModelPortal; A5CU33; -.
DR   STRING; 443906.CMM_2537; -.
DR   EnsemblBacteria; CAN02619; CAN02619; CMM_2537.
DR   KEGG; cmi:CMM_2537; -.
DR   eggNOG; ENOG4105D5N; Bacteria.
DR   eggNOG; COG0538; LUCA.
DR   HOGENOM; HOG000019858; -.
DR   KO; K00031; -.
DR   OMA; AMGMYNQ; -.
DR   Proteomes; UP000001564; 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:UP000001564};
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:CAN02619.1};
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   404 AA;  44975 MW;  C0129FC786BEB0CC CRC64;
     MEKIKVEGTV VELDGDEMTR IIWQSIKDTL IHPYLDIDLE YYDLGIEKRD ETDDQITIDA
     ANAIKKHGVG VKCATITPDE ARVEEFGLKK MWRSPNGTIR NILGGTIFRE PIIISNIPRL
     VPGWNKPIIV GRHAFGDQYR ATDFRFEGEG TLTMTFTPKD GSEPQQFEVF QSPGSGVAMG
     MYNLDDSIRD FARASLSYGL ARNYPVYLST KNTILKAYDG RFKDLFQEVF EAEYADQFAA
     AGLTYEHRLI DDMVAASLKW EGGYVWACKN YDGDVQSDTV AQGFGSLGLM TSVLTTPDGK
     VVEAEAAHGT VTRHYRQHQQ GKPTSTNPIA SIYAWTRGLA HRAKLDGNDA LKTFADTLED
     VVITTVESGK MTKDLALLVG PDQPYQTTEE FLASLAENLQ TRLA
//
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