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Database: UniProt/TrEMBL
Entry: D5UI71_CELFN
LinkDB: D5UI71_CELFN
Original site: D5UI71_CELFN 
ID   D5UI71_CELFN            Unreviewed;       422 AA.
AC   D5UI71;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN   OrderedLocusNames=Cfla_2528 {ECO:0000313|EMBL:ADG75416.1};
OS   Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / NCIB 8073 / NRS
OS   134).
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG75416.1, ECO:0000313|Proteomes:UP000000849};
RN   [1] {ECO:0000313|EMBL:ADG75416.1, ECO:0000313|Proteomes:UP000000849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 482 / DSM 20109 / NCIB 8073 / NRS 134
RC   {ECO:0000313|Proteomes:UP000000849};
RX   PubMed=21304688;
RA   Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Cellulomonas flavigena type strain
RT   (134).";
RL   Stand. Genomic Sci. 3:15-25(2010).
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; CP001964; ADG75416.1; -; Genomic_DNA.
DR   ProteinModelPortal; D5UI71; -.
DR   STRING; 446466.Cfla_2528; -.
DR   EnsemblBacteria; ADG75416; ADG75416; Cfla_2528.
DR   KEGG; cfl:Cfla_2528; -.
DR   eggNOG; ENOG4105D5N; Bacteria.
DR   eggNOG; COG0538; LUCA.
DR   HOGENOM; HOG000019858; -.
DR   KO; K00031; -.
DR   OMA; AMGMYNQ; -.
DR   OrthoDB; POG091H0JP0; -.
DR   Proteomes; UP000000849; 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:UP000000849};
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:ADG75416.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000849};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT   DOMAIN       26    413       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   NP_BIND      92     94       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   NP_BIND     327    332       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   REGION      111    117       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   METAL       269    269       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   METAL       292    292       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR000108-3}.
FT   BINDING      94     94       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING      99     99       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     126    126       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     149    149       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000108-2}.
FT   BINDING     277    277       NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT   BINDING     345    345       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000108-
FT                                4}.
FT   SITE        156    156       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
FT   SITE        229    229       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ   SEQUENCE   422 AA;  46449 MW;  BDC1602BCB0F4076 CRC64;
     MSSNLGDTPT AQEAGPRMAK IKVVGPVVEL DGDEMTRIIW QFIKDRLIHP YLDVDLRYYD
     LSIQNRDATD DQVTIDAAHA IKEHGVGVKC ATITPDEARV EEFGLKKMWV SPNGTIRNIL
     GGVVFREPII ISNIPRLVPG WNKPIIIGRH AHGDQYKATN FKVPGAGTLT LTYTPADGSE
     PIHQEVVTYP EAGGVAMGMY NFNESIRDFA RASFAYGLQR GYPVYLSTKN TILKAYDGAF
     KDIFQEVFDA EFKEQFDAAG LTYEHRLIDD MVAAAMKWEG GYVWACKNYD GDVQSDTVAQ
     GFGSLGLMTS VLMTPDGRTV EAEAAHGTVT RHYRQHQAGK PTSTNPIASI FAWTGGLKHR
     GKLDGTPEVT QFAETLEDVV ITTVESGKMT KDLALLVGKD QPWLTTEEFL AALDENLAAR
     LG
//
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