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Database: UniProt
Entry: A0A428U1K2_9HYPO
LinkDB: A0A428U1K2_9HYPO
Original site: A0A428U1K2_9HYPO 
ID   A0A428U1K2_9HYPO        Unreviewed;       592 AA.
AC   A0A428U1K2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   ORFNames=CEP52_004823 {ECO:0000313|EMBL:RSM08179.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM08179.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSM08179.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM08179.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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:RSM08179.1}.
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DR   EMBL; NKCK01000036; RSM08179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428U1K2; -.
DR   STRING; 1325735.A0A428U1K2; -.
DR   UniPathway; UPA00896; UER00863.
DR   Proteomes; UP000287144; Unassembled WGS sequence.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR   CDD; cd06558; crotonase-like; 1.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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; PF00378; ECH_1; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 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:UP000287144}.
FT   DOMAIN          5..278
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   592 AA;  64114 MW;  08542F1DC6D7CE2A CRC64;
     MTTHVRIVEV GARDGLQNIS KQVPTDVKIE LLRRLYDTGL ETIEVTSIVS PKAVPQLQDC
     RAVLTSPPVQ ALLQNASLRL PVLVPNRKGL DIARQLGVKE VAVFVSASEG FSRANINCTV
     DQGIARARLV CEEAKKFGCQ VRGYVSCIFE DPFDGLTPPT AVLKVVQTLL EMGCYEVSLG
     DTLGVGCPKN VRNLLHLLKI NNIPLDRIAG HFHDTYGQAL ANVWEAYTCG VRVFDSSVAG
     LGGCPFAPGA KGNASTEDLV YMFDRAGVYT GVNLSKLATV GAWISDKLSQ PTSSRVGAAV
     FSKERRVKKP REKSHRSLTW ERVKETDGLI VDQSGANLRI TMNRPRNGNA LTTAMIEDLT
     SIIAEVANNS SVNRIALTGS GKFFCTGMDL SKSTPVGGND DVAQAQFNRL ERLFDTIDKS
     PKVTIAALNG PAFGGGVGLA FACDLRLCVK GAKVTLSEAK LGLCPATISK YVIREWGVPF
     SREAILTARP VTPSELYAKG VVMSVVEDQT KLTEVLDSWL IKLRSVSPEA LRMSKELITS
     AWTHGGHQEQ ANTIKTLFNE MMKPSAPGHF GVSEFQAGRA VDWDAPRTRS KL
//
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