ID S7Z9R6_PENO1 Unreviewed; 502 AA.
AC S7Z9R6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN ORFNames=PDE_01899 {ECO:0000313|EMBL:EPS26959.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26959.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26959.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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 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; KB644409; EPS26959.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Z9R6; -.
DR STRING; 933388.S7Z9R6; -.
DR eggNOG; KOG1526; Eukaryota.
DR HOGENOM; CLU_023296_1_1_1; -.
DR OrthoDB; 423at2759; -.
DR PhylomeDB; S7Z9R6; -.
DR Proteomes; UP000019376; 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 Reference proteome {ECO:0000313|Proteomes:UP000019376};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT DOMAIN 101..490
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 167..169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 169
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 186..192
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 201
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 224
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 343
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 366
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 401..406
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT BINDING 419
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-4"
FT SITE 231
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
FT SITE 303
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ SEQUENCE 502 AA; 56025 MW; 8B809C149F0A5E31 CRC64;
MMNGYSLRSA SALARRSLAT PPTVALQSSS SSSVAAARLL STSSTSSALP SSRRSFSSAL
RVPRPSRVAA STRWSGSTPS LYLNQSRTMA SESTKIKVKN PVVELDGDEM TRIIWQEIRE
KLILPYLDID LKYYDLGLEY RDETNDQVTI DAAEAIKKYG VGVKCATITP DEARVEEFKL
KKMWLSPNGT IRNILGGTVF REPIIIPRIP RLVPGWNKPI VIGRHAFGDQ YRAQDRVIPG
PGKLELVYTP VGGEPERVQV YDFSSGGGVA QCQYNTDESI RGFAHASFQM ALMKGLPLYM
STKNTILKRY DGRFKDIFQE IFEKDYKKDF DAKKIWYEHR LIDDMVAQMI KSEGGFVMAL
KNYDGDVQSD IVAQGFGSLG LMTSTLVTPT GEAFESEAAH GTVTRHYREH QKGRETSTNP
IASIFAWTRG LVQRGKLDNT PDVVAFAEEL ERACVEVVND EGIMTKDLAL ACGRKDREAW
VTTNEYMNAV ERRLKANLKA RL
//
