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
//