ID A0A059DHU6_EUCGR Unreviewed; 453 AA.
AC A0A059DHU6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN ORFNames=EUGRSUZ_A02227 {ECO:0000313|EMBL:KCW90024.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW90024.1};
RN [1] {ECO:0000313|EMBL:KCW90024.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW90024.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-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}.
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DR EMBL; KK198753; KCW90024.1; -; Genomic_DNA.
DR RefSeq; XP_010055785.1; XM_010057483.2.
DR AlphaFoldDB; A0A059DHU6; -.
DR EnsemblPlants; KCW90024; KCW90024; EUGRSUZ_A02227.
DR GeneID; 104443925; -.
DR Gramene; KCW90024; KCW90024; EUGRSUZ_A02227.
DR KEGG; egr:104443925; -.
DR eggNOG; KOG2368; Eukaryota.
DR OrthoDB; 1210873at2759; -.
DR UniPathway; UPA00896; UER00863.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000138; HMG_CoA_lyase_AS.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR PANTHER; PTHR42738:SF15; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01062; HMG_COA_LYASE; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 154..421
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 40..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 47629 MW; C076CDA349F6CC8B CRC64;
MLTRRALDEV SRRGALSGRE AVSRKCDARG ALAFIGAASG ARGGDTPERS YSSSGASAAD
EVGAGDGAGE GGIRYPRRGS DQGYSVPSSR YSSIRLRNTL FNRTRGSLGW DLKATNNDSV
CDARYLSTCD YTSHCVEKNT REGGKLLGSI PRYVKIVEVG PRDGLQNEKE IVPTKVKVGL
IKMLVSSGLP VVEATSFVSP KWVPQLGDAK DVMEAIRNVE GARFPVLTPN LKGFEAAVAA
GAKEVAIFAS ASESFSKSNI NCSIEESLKR YHDVSLAAEK ASVPIRGYIS CVVGCPVEGK
VPPTKVAYVA EKLYDMGCSE ISLGDTIGVG TPGTVVPMLE AVMNVVPVDK LAVHFHDTYG
QALSNILASL QMGIATVDSS VAGLGGCPYA KGATGNVATE DVVYMLNGLG VKTNVDLGKV
MLAGDFICKH LERPSHSKTA TALSTSTAHV SKL
//
