ID A0A0C3ABP0_RHOER Unreviewed; 407 AA.
AC A0A0C3ABP0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN Name=icd {ECO:0000313|EMBL:OFV72955.1};
GN ORFNames=BS297_29110 {ECO:0000313|EMBL:KAB2581779.1}, I3517_28875
GN {ECO:0000313|EMBL:MBH5146626.1}, RERY_60340
GN {ECO:0000313|EMBL:OFV72955.1};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=1833 {ECO:0000313|EMBL:MBH5146626.1, ECO:0000313|Proteomes:UP000627573};
RN [1] {ECO:0000313|Proteomes:UP000176698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI2 {ECO:0000313|Proteomes:UP000176698};
RX PubMed=27977722; DOI=10.1371/journal.pone.0167539;
RA Khairy H., Meinert C., Wuebbeler J.H., Poehlein A., Daniel R., Voigt B.,
RA Riedel K., Steinbuechel A.;
RT "Genome and proteome analysis of Rhodococcus erythropolis MI2: elucidation
RT of the 4,4-dithiodibutyric acid catabolism.";
RL PLoS ONE 11:e0167539-e0167539(2016).
RN [2] {ECO:0000313|EMBL:OFV72955.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI2 {ECO:0000313|EMBL:OFV72955.1};
RA Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT "Genome and proteome analysis of Rhodococcus erythropolis MI2: elucidation
RT of the 4,4-dithiodibutyric acid catabolism.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAB2581779.1, ECO:0000313|Proteomes:UP000325576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S43 {ECO:0000313|EMBL:KAB2581779.1,
RC ECO:0000313|Proteomes:UP000325576};
RA Retamal-Morales G., Mehnert M., Schwabe R., Tischler D., Schloemann M.,
RA Levican G.J.;
RT "Genomic Characterization of the Arsenic-Tolerant Actinobacterium,
RT <i>Rhodococcus erythropolis</i> S43.";
RL Poromechanics V (2013) 262:660-663(2017).
RN [4] {ECO:0000313|EMBL:MBH5146626.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUR100 {ECO:0000313|EMBL:MBH5146626.1};
RA Woiski C.;
RT "Draft genome sequence of furan degrading bacterial strain FUR100.";
RL Submitted (DEC-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}.
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:MBH5146626.1}.
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DR EMBL; MRBO01000790; KAB2581779.1; -; Genomic_DNA.
DR EMBL; JAECSB010000092; MBH5146626.1; -; Genomic_DNA.
DR EMBL; LYPG01000115; OFV72955.1; -; Genomic_DNA.
DR RefSeq; WP_019747659.1; NZ_WIDN01000096.1.
DR GeneID; 57487869; -.
DR PATRIC; fig|1833.80.peg.2046; -.
DR OMA; HGTVQRH; -.
DR Proteomes; UP000176698; Unassembled WGS sequence.
DR Proteomes; UP000325576; Unassembled WGS sequence.
DR Proteomes; UP000627573; 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: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 Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT DOMAIN 9..396
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 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 310..315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 328
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 212
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ SEQUENCE 407 AA; 45213 MW; 33D18875908D0313 CRC64;
MSKIKVEGTV VELDGDEMTR IIWQFIKDKL IHPYLDVNLE YYDLGIEYRD ETDDQVTIDA
AHAIQKHGVG VKCATITPDE ARVEEFGLKK MWRSPNGTIR NILGGTIFRA PIIISNVPRL
VPGWTKPIII GRHAFGDQYR ATDFKVPGPG KVMITYTPED GSAPIEHELV NFPEEGGVVQ
GQYNFTTSIR DFARASLTYG LQQNYPVYLS TKNTILKAYD GAFKDIFQHV YETEFKAEFD
AAGLTYEHRL IDDMVASALK WEGGYVWACK NYDGDVQSDT VAQGFGSLGL MTSVLLTPDG
RTCEAEAAHG TVTRHYRQHQ QGKPTSTNPI ASIFAWTRGL EHRGKLDSTP EVIGFAQALE
DVVIKTVESG QMTKDLSMLV GGDQGYLTTE EFLGALDVNL QKAMAAK
//
