ID D1A284_THECD Unreviewed; 407 AA.
AC D1A284;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 28-FEB-2018, entry version 58.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN OrderedLocusNames=Tcur_4210 {ECO:0000313|EMBL:ACY99737.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99737.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY99737.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 /
RC Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S.,
RA Del Rio T.G., Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Detter J.C., Rohde M., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain
RT (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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 -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001738; ACY99737.1; -; Genomic_DNA.
DR RefSeq; WP_012854520.1; NC_013510.1.
DR ProteinModelPortal; D1A284; -.
DR STRING; 471852.Tcur_4210; -.
DR EnsemblBacteria; ACY99737; ACY99737; Tcur_4210.
DR KEGG; tcu:Tcur_4210; -.
DR eggNOG; ENOG4105D5N; Bacteria.
DR eggNOG; COG0538; LUCA.
DR HOGENOM; HOG000019858; -.
DR KO; K00031; -.
DR OMA; AMGMYNQ; -.
DR OrthoDB; POG091H0JP0; -.
DR BioCyc; TCUR471852:G1GG3-4188-MONOMER; -.
DR Proteomes; UP000001918; 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:UP000001918};
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:ACY99737.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT DOMAIN 9 396 Iso_dh. {ECO:0000259|SMART:SM01329}.
FT NP_BIND 75 77 NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT NP_BIND 310 315 NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT REGION 94 100 Substrate binding. {ECO:0000256|PIRSR:
FT PIRSR000108-2}.
FT METAL 252 252 Magnesium or manganese.
FT {ECO:0000256|PIRSR:PIRSR000108-3}.
FT METAL 275 275 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 260 260 NADP. {ECO:0000256|PIRSR:PIRSR000108-4}.
FT BINDING 328 328 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 212 212 Critical for catalysis.
FT {ECO:0000256|PIRSR:PIRSR000108-1}.
SQ SEQUENCE 407 AA; 45746 MW; 3BECCD64CF0EAA8C CRC64;
MPKIKVAGPV VELDGDEMTR IIWKFIKDQL ILPYLDIDLK YYDLGIQNRD ATDDQVTVDA
ANAIKKYGVG VKCATITPDE ARVEEFGLKQ MWRSPNGTIR NILGGVVFRE PIIVSNIPRL
VPGWTKPIVI GRHAHGDQYK ATDFKVPGPG TLTITYTPDD GSEPIQFEVA RYPEGGGVAM
GMYNFRKSIE DFARASFRYG LDRNYPVYLS TKNTILKAYD GMFKDVFAEI YENEFKEEFE
ARGLTYEHRL IDDMVACALK WEGGYVWACK NYDGDVQSDT VAQGFGSLGL MTSVLMTPDG
RTVEAEAAHG TVTRHYRLHQ QGKPTSTNPI ASIFAWTRGL AHRGKLDNTP EVIKFAETLE
QVCIETVESG QMTKDLALLI SKDQPWLTTQ EFLHALDVNL QKKINEK
//
