ID D4APM6_ARTBC Unreviewed; 344 AA.
AC D4APM6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Isopropylmalate dehydrogenase-like domain-containing protein {ECO:0000259|SMART:SM01329};
GN ORFNames=ARB_06194 {ECO:0000313|EMBL:EFE35237.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE35237.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE35237.1}.
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DR EMBL; ABSU01000004; EFE35237.1; -; Genomic_DNA.
DR RefSeq; XP_003015882.1; XM_003015836.1.
DR AlphaFoldDB; D4APM6; -.
DR STRING; 663331.D4APM6; -.
DR GeneID; 9526164; -.
DR KEGG; abe:ARB_06194; -.
DR eggNOG; KOG0785; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR OMA; DSFVMGE; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000008866; 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:UP000008866}.
FT DOMAIN 7..340
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 344 AA; 36573 MW; 1297B0C25A1CC14F CRC64;
MAARTLRIGQ LIPKAASSLG LKFSFVDLDA GYDTFLRTKT ALPDKTVETL KKECDGALFG
AVSSPSTKVA GYSSPIVALR KKLDLYANVR PVKTTAGANA SVRPIDLVIV RENTEDLYVK
EEKTYDTPNG KVAEAIKRIS ENASFRIGTM AGEIALRRQK IRQAQSANTT TASPMVTITH
KSNVLSQSDG LFRETCRKAL ANEKFSGVNV EEQIVDSMVY KLFRQPSYYD VIVAPNLYGD
ILSDGAAALV GSLGLVPSAN VGDGFAIGEP CHGSAPDIEG KGIANPIATI RSTALMLEFL
GEGAAAAKIY AAVDANLDEG KLLSPDLGGK ATTAEVLEDV LKKL
//
