ID A8PTA7_MALGO Unreviewed; 239 AA.
AC A8PTA7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha domain-containing protein {ECO:0000259|Pfam:PF00330};
GN ORFNames=MGL_0394 {ECO:0000313|EMBL:EDP45405.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP45405.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP45405.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
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:EDP45405.1}.
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DR EMBL; AAYY01000001; EDP45405.1; -; Genomic_DNA.
DR RefSeq; XP_001732619.1; XM_001732567.1.
DR AlphaFoldDB; A8PTA7; -.
DR STRING; 425265.A8PTA7; -.
DR GeneID; 5856925; -.
DR KEGG; mgl:MGL_0394; -.
DR VEuPathDB; FungiDB:MGL_0394; -.
DR InParanoid; A8PTA7; -.
DR OrthoDB; 3266779at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF2; HOMOCITRATE DEHYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00330; Aconitase; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT DOMAIN 61..204
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 239 AA; 25703 MW; 8D0AE2A8547C69ED CRC64;
MYILRVCRGM QNCWRSSRAY EHFCKGAPWT LAEKILYTHL LNPAVDLAGA GADPSKVRGA
RYLRLGVDRL AMQDASAQMA LLQFMTCGMS QSAVPASVHC DHLIQAYEGA QADLQRSLET
QHEVFAFLES ACRKYGIEFW RPGSGIIHQI VLENYAAPGL LMLGTDSHTP NASGLGCLAI
GVGGADAVDA LTATPLGVAC AESLGRASAW KAVAVVLGQG CDSAPDGRAY RAWRHRLHC
//
