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Database: UniProt
Entry: M5FNM6_DACPD
LinkDB: M5FNM6_DACPD
Original site: M5FNM6_DACPD 
ID   M5FNM6_DACPD            Unreviewed;       362 AA.
AC   M5FNM6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   03-MAY-2023, entry version 32.
DE   SubName: Full=Isocitrate/isopropylmalate dehydrogenase {ECO:0000313|EMBL:EJT97695.1};
GN   ORFNames=DACRYDRAFT_25045 {ECO:0000313|EMBL:EJT97695.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT97695.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJT97695.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT97695.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR   EMBL; JH795876; EJT97695.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5FNM6; -.
DR   STRING; 1858805.M5FNM6; -.
DR   HOGENOM; CLU_031953_0_1_1; -.
DR   OMA; DSFVMGE; -.
DR   OrthoDB; 143577at2759; -.
DR   Proteomes; UP000030653; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF48; HOMOISOCITRATE DEHYDROGENASE, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT   DOMAIN          17..358
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   362 AA;  38981 MW;  9EFF1988714C24FE CRC64;
     MVAVLRGAAS LGLKKLRVGM IPADGVGREV LPAAQRILEA LGPSIPKPEF THLDAGWEYF
     TRHGVALPEE TADALQNDCD CALFGAVGSP THRVTGYSSP IVALRKKLSL YANVRPVHSI
     EGLDPRPVDM VIVRENTECL YIKQETSSHS EENGREARAT RLITERASKQ IGRMAFRIAL
     SRAKPDHPAS LTIVHKSNVL QLTDGLFREC VRSVMKENEE WSDGSKIAVG EQIVDSMVYR
     MFREPEAFDV VVAPNLYGDI LSDAAAALVG SLGLVPSVNA GDTFVMGEPV HGTAPDIAGL
     GIVNPIAAIR SAGLMLHHLG YIEPAQKVED AVVSVLKEGV RTRDLGGNAS TEEVVAAIEK
     RL
//
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