ID A0A087FMW6_KLEVA Unreviewed; 416 AA.
AC A0A087FMW6; A0A0J4RNM0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446};
DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446};
GN Name=icd_1 {ECO:0000313|EMBL:STS89786.1};
GN Synonyms=icd {ECO:0000313|EMBL:QNP23046.1};
GN ORFNames=AN2335V1_1504 {ECO:0000313|EMBL:CAH6022244.1}, CWM98_05310
GN {ECO:0000313|EMBL:PLP47916.1}, CWN47_24190
GN {ECO:0000313|EMBL:PLM91962.1}, IAP99_16570
GN {ECO:0000313|EMBL:QNP23046.1}, NCTC9177_03672
GN {ECO:0000313|EMBL:STS89786.1}, NCTC9178_04149
GN {ECO:0000313|EMBL:VTO21950.1}, NUKP37_06480
GN {ECO:0000313|EMBL:GKJ86730.1}, SAMEA3729809_02282
GN {ECO:0000313|EMBL:SXF93562.1};
OS Klebsiella variicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=244366 {ECO:0000313|EMBL:PLM91962.1, ECO:0000313|Proteomes:UP000234412};
RN [1] {ECO:0000313|Proteomes:UP000234412, ECO:0000313|Proteomes:UP000234473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5 {ECO:0000313|EMBL:PLP47916.1,
RC ECO:0000313|Proteomes:UP000234473}, and A8
RC {ECO:0000313|EMBL:PLM91962.1, ECO:0000313|Proteomes:UP000234412};
RA Han C.G.;
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000234412, ECO:0000313|Proteomes:UP000234473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5 {ECO:0000313|EMBL:PLP47916.1,
RC ECO:0000313|Proteomes:UP000234473}, and A8
RC {ECO:0000313|EMBL:PLM91962.1, ECO:0000313|Proteomes:UP000234412};
RA Yang Y., Bicalho R.;
RT "Genomic study of Klebsiella pneumoniae.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:STS89786.1, ECO:0000313|Proteomes:UP000254545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC9177 {ECO:0000313|EMBL:STS89786.1,
RC ECO:0000313|Proteomes:UP000254545};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:SXF93562.1, ECO:0000313|Proteomes:UP000258928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EuSCAPE_TR218 {ECO:0000313|EMBL:SXF93562.1,
RC ECO:0000313|Proteomes:UP000258928}, and NCTC9178
RC {ECO:0000313|EMBL:VTO21950.1, ECO:0000313|Proteomes:UP000309475};
RG Pathogen Informatics;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QNP23046.1, ECO:0000313|Proteomes:UP000516181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP2757 {ECO:0000313|EMBL:QNP23046.1,
RC ECO:0000313|Proteomes:UP000516181};
RA Zhang X.;
RT "Complete genome sequence of Klebsiella pneumoniae KP2757.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:GKJ86730.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUKP-37 {ECO:0000313|EMBL:GKJ86730.1};
RX PubMed=35797348; DOI=10.1111/jam.15701;
RA Nonogaki R., Iijima A., Kawamura K., Kayama S., Sugai M., Yagi T.,
RA Arakawa Y., Doi Y., Suzuki M.;
RT "PCR-based ORF typing of Klebsiella pneumoniae for rapid identification of
RT global clones and transmission events.";
RL J. Appl. Microbiol. 133:2050-2062(2022).
RN [7] {ECO:0000313|EMBL:CAH6022244.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=0 {ECO:0000313|EMBL:CAH6022244.1};
RA Alioto T., Alioto T., Gomez Garrido J.;
RL Submitted (MAY-2022) 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|ARBA:ARBA00023554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR604439-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; CAJOXS020000001; CAH6022244.1; -; Genomic_DNA.
DR EMBL; BQTA01000001; GKJ86730.1; -; Genomic_DNA.
DR EMBL; PIDP01001083; PLM91962.1; -; Genomic_DNA.
DR EMBL; PICB01000163; PLP47916.1; -; Genomic_DNA.
DR EMBL; CP060807; QNP23046.1; -; Genomic_DNA.
DR EMBL; UGKR01000003; STS89786.1; -; Genomic_DNA.
DR EMBL; UKAS01000006; SXF93562.1; -; Genomic_DNA.
DR EMBL; LR588409; VTO21950.1; -; Genomic_DNA.
DR RefSeq; WP_008806032.1; NZ_WUQO01000001.1.
DR GeneID; 69735804; -.
DR KEGG; kpk:A593_20180; -.
DR KEGG; kvd:KR75_17855; -.
DR KEGG; kvq:SP68_24265; -.
DR OMA; CVRPCRY; -.
DR Proteomes; UP000234412; Unassembled WGS sequence.
DR Proteomes; UP000234473; Unassembled WGS sequence.
DR Proteomes; UP000254545; Unassembled WGS sequence.
DR Proteomes; UP000258928; Unassembled WGS sequence.
DR Proteomes; UP000309475; Chromosome.
DR Proteomes; UP000516181; Chromosome.
DR Proteomes; UP000789617; Unassembled WGS sequence.
DR Proteomes; UP001060507; 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: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; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00183; prok_nadp_idh; 1.
DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW ECO:0000256|RuleBase:RU004446};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3, ECO:0000256|RuleBase:RU004446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004446};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:PLM91962.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000516181};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 28..412
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 104
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 339..345
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 352
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 391
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 395
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 160
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 230
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 100
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 242
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 416 AA; 45754 MW; 2DCC427CEB1701E5 CRC64;
MESKVVVPAE GQKITLQNGK LNVPHNPIIP FIEGDGIGVD VTPAMLKVVD AAVEKAYKGE
RKISWMEVYT GEKSTQVYGQ DVWLPAETLD LIRDYRVAIK GPLTTPVGGG IRSLNVALRQ
ELDLYVCLRP VRYYQGTPSP VKHPELTDMV IFRENSEDIY AGIEWKADSA EADKVIKFLR
DEMGVKKIRF PEHCGIGIKP CSEEGTKRLV RAAIEYAITN DRDSLTLVHK GNIMKFTEGA
FKDWGYQLAR EEFGGELIDG GPWVKIKNPN TGKEIVVKDV IADAFLQQIL LRPAEYDVIA
CMNLNGDYIS DALAAQVGGI GIAPGANIGD ECALFEATHG TAPKYAGQDK VNPGSIILSA
EMMLRHMQWF EAADLIVKGM EGAIAAKTVT YDFERLMEGA KLLKCSEFGD AIIANM
//
