ID A0A0D5YEU5_ACIBA Unreviewed; 418 AA.
AC A0A0D5YEU5; B0VCP0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, 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 {ECO:0000313|EMBL:AKA30827.1};
GN ORFNames=ABUW_1074 {ECO:0000313|EMBL:AKA30827.1}, F2P40_17565
GN {ECO:0000313|EMBL:MQR51107.1}, HIN86_05045
GN {ECO:0000313|EMBL:QJF34629.1};
OS Acinetobacter baumannii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=470 {ECO:0000313|EMBL:AKA30827.1, ECO:0000313|Proteomes:UP000032746};
RN [1] {ECO:0000313|EMBL:AKA30827.1, ECO:0000313|Proteomes:UP000032746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB5075-UW {ECO:0000313|EMBL:AKA30827.1,
RC ECO:0000313|Proteomes:UP000032746};
RX PubMed=25845845;
RA Gallagher L.A., Ramage E., Weiss E.J., Radey M., Hayden H.S., Held K.G.,
RA Huse H.K., Zurawski D.V., Brittnacher M.J., Manoil C.;
RT "Resources for Genetic and Genomic Analysis of Emerging Pathogen
RT Acinetobacter baumannii.";
RL J. Bacteriol. 197:2027-2035(2015).
RN [2] {ECO:0000313|Proteomes:UP000032746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB5075-UW {ECO:0000313|Proteomes:UP000032746};
RA Gallagher L.A., Hayden H.S., Weiss E.J., Hager K.R., Ramage E., Radey M.R.,
RA Bydalek R., Manoil C., Miller S.I., Brittnacher M.J.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MQR51107.1, ECO:0000313|Proteomes:UP000461234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABS103 {ECO:0000313|EMBL:MQR51107.1,
RC ECO:0000313|Proteomes:UP000461234};
RA Douraghi M., Aris P., Kenyon J., Hamidian M.;
RT "Genetic environment of the oxa23 gene and comparative analysis of
RT carbapenem resistant Acinetobacter baumannii isolates belonging to global
RT clone 1, lineage 2 recovered in a burns hospital outbreak in 2012-2013.";
RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QJF34629.1, ECO:0000313|Proteomes:UP000501210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ab-B004d-c {ECO:0000313|EMBL:QJF34629.1,
RC ECO:0000313|Proteomes:UP000501210};
RA Ayibieke A., Saito R.;
RT "Whole-genome sequence analysis of carbapanemase producing Acinetobacter
RT baumannii isolates from Ghana.";
RL Submitted (APR-2020) 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; CP008706; AKA30827.1; -; Genomic_DNA.
DR EMBL; WIOC01000030; MQR51107.1; -; Genomic_DNA.
DR EMBL; CP051875; QJF34629.1; -; Genomic_DNA.
DR RefSeq; WP_000542117.1; NZ_WYAS01000003.1.
DR PATRIC; fig|470.1294.peg.3070; -.
DR OMA; CVRPCRY; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000032746; Chromosome.
DR Proteomes; UP000461234; Unassembled WGS sequence.
DR Proteomes; UP000501210; 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: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 Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 30..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 242
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 418 AA; 45635 MW; A094407343ACB50F CRC64;
MGYQKIVVPA DGDKITVKAD LSLNVPNHPI IPFIEGDGIG VDITPAMKKV VDAAILKAYG
GKRSIEWMEV YCGEKANKIY GTYMPEETFE ALREFVVSIK GPLTTPVGGG IRSLNVALRQ
ELDLYVCVRP VRWFQGVPSP VQHPELTDMV IFRENSEDIY AGIEWKADSE EAKKVIKFLQ
EEMGVTKIRF PEGCGIGIKP VSKEGTQRLV RKAIQFAIDN DKPSVTLVHK GNIMKYTEGA
FKEWGYELAL DRFGGELIDG GPWVKIKNPK NGKDIIIKDV IADAFLQQIL MRPADYSVIA
TLNLNGDYIS DALAAEVGGI GIAPGANIGG AIAVYEATHG TAPKYAGQDK VNPGSIILSA
EMMLRDMGWI EAADLIIKGI SGAIAAKTVT YDFERLMPGA TLLRCSEFGD AIIQHMED
//
