ID A0A094D3F9_9PEZI Unreviewed; 918 AA.
AC A0A094D3F9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
GN ORFNames=V493_02418 {ECO:0000313|EMBL:KFY29327.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY29327.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY29327.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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|ARBA:ARBA00001946};
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:KFY29327.1}.
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DR EMBL; JPJV01000942; KFY29327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094D3F9; -.
DR STRING; 1420906.A0A094D3F9; -.
DR HOGENOM; CLU_014363_0_0_1; -.
DR OrthoDB; 423at2759; -.
DR Proteomes; UP000029327; Unassembled WGS sequence.
DR GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
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:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR032742; Iec3.
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; PF14612; Ino80_Iec3; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000029327}.
FT DOMAIN 518..906
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 101703 MW; 9AE0D5D636225C48 CRC64;
MTESELPPLK AMDESNADEH DASKETYRSF KKKYRKMRHQ FDQKMNLSRS LYKQEQEAAE
TSRRLALEND GLLELLLDMN NSPNLPSAQR IDLSATAPNV SLAPLPLLFP PTPATSPDQK
GMTRGQESYN KLHAYMHSSM TDKRSSAPRP QKSLASLMAN VPHRPYEVTT VPPSVYNVPG
VPPDIAKDLE IGPDKPEPVA YLSADRIDEH CALVDANLDL PTEPTLYTSN PSFVPAPLHL
SDKDLEFKNP VSVYNWLREH EPKIFLQDDE PADLAEKAVS RPGALRGAGK RAAIAAPTRP
DVVEFVEEDG LKYFASISDQ YAKDRTASGG KRKRGPTDED GGYRPKGGSS RAAKKKRGEG
RASTGSRKER EKAEKEEDAD VDVDMADEGL AGLIRLTTTL QNLHLFSTPP TSSPSPQLPY
PTIVNDIGGR KSGRGSELTY KINFLVRVSA SEGIVSKTST IVLPSPLGFI PPSSLSTAHF
PAGNLARDRT PEAIPLCSRP TTDGATMTVF QKIKVKNPVV ELDGDEMTRI IWQDIKDKFI
HPYLDIDLKY YDLGLEYRDE TNDQVTIDAA EAIKKYSVGV KCATITPDEA RVEEFKLKQM
WLSPNGTIRN ALGGTVFREP IVIPRIPRLV PGWKKPIIIG RHAFGDQYRA KDTVIKGKGK
LSMVFTPEGG KPEEIEVYNF NGGGVAQTQY NTDESISGFA HASFKLALSK SLPLYMSTKN
TILKKYDGRF KDIFQEIYET TYAKEFDAKK IWYEHRLIDD MVAQMMKSSG GYIMALKNYD
GDVQSDIVAQ GFGSLGLMTS VLITPDGKSF ESEAAHGTVT RHYREHQKGN ETSTNPIASI
FAWTRGLIQR GTLDNTPEVV SFAEALEQAC IDTVDVDGIM TKDLALACGQ TSRESYVTTK
KYMEAVERRM QKALKASL
//
