ID A0A1D7ZGE6_9BURK Unreviewed; 742 AA.
AC A0A1D7ZGE6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN Name=icd_1 {ECO:0000313|EMBL:VBB12959.1};
GN ORFNames=BBJ41_16185 {ECO:0000313|EMBL:AOR68942.1}, BSTAB16_3128
GN {ECO:0000313|EMBL:VBB12959.1};
OS Burkholderia stabilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=95485 {ECO:0000313|EMBL:AOR68942.1, ECO:0000313|Proteomes:UP000094154};
RN [1] {ECO:0000313|EMBL:AOR68942.1, ECO:0000313|Proteomes:UP000094154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-67 {ECO:0000313|EMBL:AOR68942.1,
RC ECO:0000313|Proteomes:UP000094154};
RA Bugrysheva J.V., Cherney B., Sue D., Conley A.B., Rowe L.A., Knipe K.M.,
RA Frace M.A., Loparev V.N., Avila J.R., Anderson K., Hodge D.R., Pillai S.P.,
RA Weigel L.M.;
RT "Complete Genome Sequence of the Burkholderia stabilis Type Strain (ATCC
RT BAA-67).";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VBB12959.1, ECO:0000313|Proteomes:UP000268684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:VBB12959.1};
RA Seth-Smith MB H.;
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC Evidence={ECO:0000256|PIRNR:PIRNR009407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR009407-3};
CC -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC {ECO:0000256|PIRNR:PIRNR009407}.
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DR EMBL; CP016442; AOR68942.1; -; Genomic_DNA.
DR EMBL; LR025742; VBB12959.1; -; Genomic_DNA.
DR RefSeq; WP_069747244.1; NZ_LR025742.1.
DR GeneID; 71055594; -.
DR KEGG; bstl:BBJ41_16185; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000094154; Chromosome 1.
DR Proteomes; UP000268684; Chromosome i.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR NCBIfam; TIGR00178; monomer_idh; 1.
DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF03971; IDH; 1.
DR PIRSF; PIRSF009407; IDH_monmr; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 83..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 133..140
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 136
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 548
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 549
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 553
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 585..586
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 590
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 601..603
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 650
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 256
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 421
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 742 AA; 79987 MW; 06B354A107C685BF CRC64;
MSTSPKIIYT LTDEAPALAT YSLLPIVKAF TRSSGVAVET RDISLAGRII AAFADVLPSE
QKGSDDLAEL GQLTLKPEAN IIKLPNISAS VPQLKAAIVE LQAQGYKLPA YPEDPSTDEE
KAVKARYDKI KGSAVNPVLR EGNSDRRAPL SVKNYARKHP HKMGAWKATS KAHVAHMSEG
DFYGSEKSAL IADAGSVKIE LTTADGVKKV LKEKTAVKAG EIIDASVMSR KALRSFIEAQ
IADAKAQDVL FSVHLKATMM KVSDPILFGH FVSVFYRDAL AKHADVLAQA GFNPNNGIGD
LYARLKDLPA DTREAIEADV KAEYAVRPRL AMVNSDKGIT NLHVPSDVIV DASMPAMIRD
SGGMWGPDGQ LYDAKAVIPD RCYAGVYQAV IEDCKQHGAF DPVTMGSVPN VGLMAQAAEE
YGSHDKTFQI PADGVVRVTD EAGNVLLEHA VESGDIWRMC QTKDAPVQDW VKLAVNRARA
TGAPAVFWLD PARAHDAQII AKVERYLKDH DTNGLDIRIL TPVDATRFSL ERIRAGKDTI
SVTGNVLRDY LTDLFPIMEL GTSAKMLSIV PLMAGGGMFE TGAGGSAPKH VQQFVEEGFL
RWDSLGEFLA LAASLEHLGH AYQNPKAVVL AKTLDQATGK FLDENKSPAR KVGGLDNRGS
HFYLCLYWAQ ALAEQTEDAA LKAQFEGVAK ALSDSEARIL EELAGAQGKP QAIGGYYRPN
VDLTSQAMRP SATLNGIVDA VA
//
