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Database: UniProt
Entry: A0A0C9ZNS4_9AGAM
LinkDB: A0A0C9ZNS4_9AGAM
Original site: A0A0C9ZNS4_9AGAM 
ID   A0A0C9ZNS4_9AGAM        Unreviewed;       440 AA.
AC   A0A0C9ZNS4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   ORFNames=PISMIDRAFT_678692 {ECO:0000313|EMBL:KIK23962.1};
OS   Pisolithus microcarpus 441.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK23962.1, ECO:0000313|Proteomes:UP000054018};
RN   [1] {ECO:0000313|EMBL:KIK23962.1, ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|EMBL:KIK23962.1,
RC   ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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; KN833721; KIK23962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9ZNS4; -.
DR   STRING; 765257.A0A0C9ZNS4; -.
DR   HOGENOM; CLU_022138_3_0_1; -.
DR   OrthoDB; 1210873at2759; -.
DR   UniPathway; UPA00896; UER00863.
DR   Proteomes; UP000054018; 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; 1.
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:UP000054018}.
FT   DOMAIN          105..378
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          421..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   440 AA;  46848 MW;  BD1978FBD29D1254 CRC64;
     MIHRQGIPAF KNPFDGDGWP WTGYMAPCLA VTPTAISGMI RTVVGLFRGA SQTRTGVGSE
     LTEINCLSTA TRSMFRSYSQ VVRRASLRRG MLSRHPPSRP ASDFVRIVEV GPRDGLQNEQ
     RPIAPAIKAE LINKLARAGM RNIEVGSFVS PKWVPQMAGT SEVLSLIEPV ANASYSVLVP
     NRKGLDDVLN LLSRSPSPPP ITEIAVFTSA TDAFSKANTN VTVAESLARL APVVRAALDA
     GLRVRGYVSV IITCPYSGRV DPRRVREVAR ELLEMGCYEV SLGDTTGAGT PESVRAVLEE
     VTKDIGVGQL AGHFHDTNGT ALANIKTALD FGLRSFDASV GGLGGCPYSP GATGNVATED
     VVYALTGGDS YGDVGEPYSD TPVVQGPAWD VGPVSLPLLA DTGSWISSVL KRETTSRAGK
     ALLARKERER RLSESAQAKL
//
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