ID A0A099G1N9_9RHOB Unreviewed; 404 AA.
AC A0A099G1N9; A0A099GHA6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN ORFNames=HGN31_07560 {ECO:0000313|EMBL:QJD16741.1}, IX56_09305
GN {ECO:0000313|EMBL:KGJ22240.1}, SAMN05444276_10511
GN {ECO:0000313|EMBL:SDX34588.1};
OS Paracoccus sanguinis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ22240.1, ECO:0000313|Proteomes:UP000029858};
RN [1] {ECO:0000313|EMBL:KGJ22240.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22240.1,
RC ECO:0000313|Proteomes:UP000029858};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ22240.1, ECO:0000313|Proteomes:UP000029858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5503 {ECO:0000313|EMBL:KGJ22240.1,
RC ECO:0000313|Proteomes:UP000029858};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SDX34588.1, ECO:0000313|Proteomes:UP000182944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29303 {ECO:0000313|EMBL:SDX34588.1,
RC ECO:0000313|Proteomes:UP000182944};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QJD16741.1, ECO:0000313|Proteomes:UP000503485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM2164 {ECO:0000313|EMBL:QJD16741.1,
RC ECO:0000313|Proteomes:UP000503485};
RA Wu V.;
RT "Genome-Wide Identification of 5-Methylcytosine Sites in Bacterial Genomes
RT By High-Throughput Sequencing of MspJI Restriction Fragments.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:QJD16741.1, ECO:0000313|Proteomes:UP000503485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM2164 {ECO:0000313|EMBL:QJD16741.1,
RC ECO:0000313|Proteomes:UP000503485};
RA Fomenkov A., Anton B.P., Roberts R.J.;
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|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 -!- 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 ECO:0000256|PIRNR:PIRNR000108}.
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DR EMBL; JRKQ01000041; KGJ22240.1; -; Genomic_DNA.
DR EMBL; CP051542; QJD16741.1; -; Genomic_DNA.
DR EMBL; FNNA01000005; SDX34588.1; -; Genomic_DNA.
DR RefSeq; WP_036709531.1; NZ_JRKQ01000041.1.
DR STRING; 1545044.SAMN05444276_10511; -.
DR KEGG; psan:HGN31_07560; -.
DR OrthoDB; 9765655at2; -.
DR Proteomes; UP000029858; Unassembled WGS sequence.
DR Proteomes; UP000182944; Unassembled WGS sequence.
DR Proteomes; UP000503485; 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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000108};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000108};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000108};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000108};
KW Reference proteome {ECO:0000313|Proteomes:UP000029858};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT DOMAIN 9..394
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 75..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 77
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 94..100
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 109
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 132
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 258
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 308..313
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 326
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT SITE 139
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
FT SITE 210
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ SEQUENCE 404 AA; 45258 MW; 7C1D7FD41C827CAD CRC64;
MTKIKVDNPV VELDGDEMTR IIWDFIKQKL ILPYLDIDLK YYDLGIEERD RTEDQITVDA
ANAIKQYGVG VKCATITPDE ARVEEFGLKK MWKSPNGTIR NILGGVIFRE PIICKNVPRL
VPGWTQPIIV GRHAFGDQYK ATDFRFPGKG TLTIRFVGED GETIEHEVFQ APSSGVAMAM
YNLDDSIRDF ARASMNYGLN RGYPVYLSTK NTILKAYDGR FKDLFQEVFD AEFADKFKAA
GITYEHRLID DMVASALKWS GGYVWACKNY DGDVQSDTVA QGFGSLGLMT SVLMTPDGKT
VESEAAHGTV TRHYRQHQAG KETSTNSIAS IFAWTGGLKH RAKLDGNDQL KRFAETLERV
TVQAVEDGHM TKDLAMLVGP DQKWLTTMGY LEKVDEYLNK ALAG
//
