ID A0A0D2KU65_9EURO Unreviewed; 368 AA.
AC A0A0D2KU65;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN ORFNames=Z520_03979 {ECO:0000313|EMBL:KIY00294.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY00294.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY00294.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY00294.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57288; EC=4.1.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001651};
CC -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC methylglutaryl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00005143}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
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DR EMBL; KN848067; KIY00294.1; -; Genomic_DNA.
DR RefSeq; XP_016634416.1; XM_016774489.1.
DR AlphaFoldDB; A0A0D2KU65; -.
DR STRING; 1442371.A0A0D2KU65; -.
DR GeneID; 27709725; -.
DR VEuPathDB; FungiDB:Z520_03979; -.
DR OrthoDB; 1210873at2759; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR PANTHER; PTHR42738:SF11; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 2.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411}.
FT DOMAIN 31..339
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 39610 MW; 0508919259E5541A CRC64;
MKRLIGSLPR TRSRPPFRSF STSRQCLADH VRIVEVGPRD GLQNEKSTIS LDTKLELIRR
LAQTGVTHME AGSFVPAKWV PQMASTAEIL ESILTQPPPA PHGIAYNYLV PNIRGLENLL
KTFQAKGAQN PSGYPTPPPS PEPEQSQGQS SSAQSENSTE ISLFAAATET FSQKNTNCSI
AESLERSKPI MELAKQHNIR VRGYVSVALG CPYEGPDVNP HKVAEITATL LEMGCDEVSV
ADTTGMGTAP RTRKLLQTLK EAGILDEDLA LHFHDTYGMA LVNTVVGLEH GVRIFDSSVG
GLGGCPYSKG ATGNVATEDL LHLVHSLGCE TGVDMVKMAE IGQWITAQLG RANDSRAGKA
TLARLKDS
//
