ID B0YBY9_ASPFC Unreviewed; 412 AA.
AC B0YBY9;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN ORFNames=AFUB_088300 {ECO:0000313|EMBL:EDP48120.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP48120.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP48120.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499601; EDP48120.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YBY9; -.
DR EnsemblFungi; EDP48120; EDP48120; AFUB_088300.
DR VEuPathDB; FungiDB:AFUB_088300; -.
DR HOGENOM; CLU_022138_3_0_1; -.
DR PhylomeDB; B0YBY9; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000001699; 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:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EDP48120.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 22..295
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 371..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 44384 MW; 698F5E577E301EF3 CRC64;
MLVSLRSAAH EYPGTMTISK AVRIVEVGPR DGLQNIKEPV PTSVKLELIQ RLRATGLRTI
ELTSVVSPKA IPQLADGRDV LGNEFIRQLQ GTPDLRLPVL VPNVKGLDIA IEHGAKEVAV
FVSATEGFSK ANINCTVQQG LERAKAVAKK ATECGITVRG YVSCIFSDPF DGPTEPSAVL
HCVQELLDMG CYEVSLGDTL GVGNPGKVRS LLHYLADHHI PLDKMAGHFH DTYGQAVANV
WEAYNCGVRV FDSSVGGLGG CPYAPGAKGN VATEDLVYMF ETAGINTGVD LRKLVETGVW
ISRRLSKTNA SRAGTALAAK YGLVPFKRSS SSRTTTKNQI FWTVVKDPNG SLAYRSGVNV
KPIIDRLKRR NVFTSSGSSK TPRPTPPSSD SSSQEREGSS LQAWISTRTV HL
//
