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Database: UniProt
Entry: W9ZKI7_9EURO
LinkDB: W9ZKI7_9EURO
Original site: W9ZKI7_9EURO 
ID   W9ZKI7_9EURO            Unreviewed;       400 AA.
AC   W9ZKI7;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   ORFNames=A1O1_00137 {ECO:0000313|EMBL:EXJ95019.1};
OS   Capronia coronata CBS 617.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ95019.1, ECO:0000313|Proteomes:UP000019484};
RN   [1] {ECO:0000313|EMBL:EXJ95019.1, ECO:0000313|Proteomes:UP000019484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ95019.1,
RC   ECO:0000313|Proteomes:UP000019484};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia coronata CBS 617.96.";
RL   Submitted (MAR-2013) 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}.
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:EXJ95019.1}.
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DR   EMBL; AMWN01000001; EXJ95019.1; -; Genomic_DNA.
DR   RefSeq; XP_007719248.1; XM_007721058.1.
DR   AlphaFoldDB; W9ZKI7; -.
DR   STRING; 1182541.W9ZKI7; -.
DR   GeneID; 19155047; -.
DR   eggNOG; KOG2368; Eukaryota.
DR   HOGENOM; CLU_022138_3_0_1; -.
DR   OrthoDB; 1210873at2759; -.
DR   UniPathway; UPA00896; UER00863.
DR   Proteomes; UP000019484; 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; 2.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:EXJ95019.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019484}.
FT   DOMAIN          38..370
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   400 AA;  42693 MW;  09BF3411EFD80E92 CRC64;
     MKSLVARISP SARRTTSTTT PRFLRPFSTS RHHAADHVRI VEVGPRDGLQ NEKSTIPLDT
     KLELIRRLAQ TGVTHMEAGS FVPAKWVPQM ASTAEILEKI LTDPPPAPHG IAYNYLVPNI
     RGMESLVKIF QTQNAQNPTG LPTPPPSPSL RPESSTTSSN PDELSTSGTS PSTTSTGEST
     STSASTSNST EISLFAAATE TFSQKNTNCS IAESLSRCRP IIDLAKQHSI RVRGYVSVAL
     GCPYEGPDVD PHKVAEITAS LLEMGCDEVS VADTTGMGTA PRTLKLLETL KDAGILNEDL
     ALHFHDTYGM ALVNTVVGLE HGVRVFDSSV GGLGGCPYSK GATGNVATED LLHLLHSLGC
     ETGVDLVKMA EIGEWITQKL GRKNDSRAGK AVLARLKDQS
//
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