ID A0A0W0Y0W5_9GAMM Unreviewed; 418 AA.
AC A0A0W0Y0W5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:KTD50663.1};
GN ORFNames=Lqui_1229 {ECO:0000313|EMBL:KTD50663.1};
OS Legionella quinlivanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD50663.1, ECO:0000313|Proteomes:UP000054618};
RN [1] {ECO:0000313|EMBL:KTD50663.1, ECO:0000313|Proteomes:UP000054618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD50663.1,
RC ECO:0000313|Proteomes:UP000054618};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD50663.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNYS01000007; KTD50663.1; -; Genomic_DNA.
DR RefSeq; WP_058507354.1; NZ_UGOX01000001.1.
DR AlphaFoldDB; A0A0W0Y0W5; -.
DR STRING; 45073.Lqui_1229; -.
DR PATRIC; fig|45073.5.peg.1296; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000054618; 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 Reference proteome {ECO:0000313|Proteomes:UP000054618};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 30..414
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 341..347
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 393
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 397
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 162
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 232
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 102
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 244
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 418 AA; 45837 MW; 5092DB577922F105 CRC64;
MTFEKIKVPA NGQAITVAPD FSLQVPDHPI IPFIEGDGIG VDVTPAMRMV VDAAVEKAYG
DKRKIAWMEV YAGEKATRVY GENHWLPKET LQAISEFVIG IKGPLTTPVG GGIRSLNVAI
RQDLDLYTCL RPVRYFQGTP SPLKEPWKTD MVIFRENSED IYAGIEWQAD SVEAKKVIRF
LQEDMGVKKI RFPDHCGIGI KPVSQQGTAR LVKAAIQYAI DNNRDSVTLV HKGNIMKFTE
GAFKDWGYQV ARECFSATEY QGGPWLHFKN PKTGKDIIVK DVIADAFLQQ ILLRPDEYSV
IVTLNLNGDY ISDALAAQVG GIGIAPGANM ADAIAVFEAT HGTAPKYAGQ DKVNPGSLIL
SAEMMLRHLG WTEAADLIIK GTEGAIEAKT VTYDFARLMS GATEVSCSGF AKEIINHM
//
