HMGCL_ARATH
ID HMGCL_ARATH Reviewed; 468 AA.
AC O81027; Q8L7K2; Q9FPE2;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Hydroxymethylglutaryl-CoA lyase, mitochondrial;
DE Short=HL;
DE Short=HMG-CoA lyase;
DE EC=4.1.3.4;
DE AltName: Full=3-hydroxy-3-methylglutarate-CoA lyase;
GN Name=HMGCL; OrderedLocusNames=At2g26800; ORFNames=F12C20.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=14764908; DOI=10.1104/pp.103.035675;
RA Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.;
RT "Lipoic acid-dependent oxidative catabolism of alpha-keto acids in
RT mitochondria provides evidence for branched-chain amino acid catabolism in
RT Arabidopsis.";
RL Plant Physiol. 134:838-848(2004).
CC -!- FUNCTION: Involved in the catabolism of branched amino acids such as
CC leucine. {ECO:0000305}.
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 -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
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.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC O81027; Q84MC7: PYL9; NbExp=3; IntAct=EBI-4434127, EBI-2349513;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14764908}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O81027-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O81027-2; Sequence=VSP_038469;
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
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DR EMBL; AC005168; AAC32247.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07888.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07890.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62277.1; -; Genomic_DNA.
DR EMBL; AF327420; AAG42010.1; -; mRNA.
DR EMBL; AF349521; AAK15568.1; -; mRNA.
DR EMBL; AY128409; AAM91612.1; -; mRNA.
DR EMBL; BT000081; AAN15400.1; -; mRNA.
DR PIR; T02655; T02655.
DR RefSeq; NP_001324446.1; NM_001336085.1. [O81027-1]
DR RefSeq; NP_565629.1; NM_128237.3. [O81027-1]
DR RefSeq; NP_850087.1; NM_179756.4. [O81027-2]
DR AlphaFoldDB; O81027; -.
DR SMR; O81027; -.
DR BioGRID; 2573; 7.
DR IntAct; O81027; 7.
DR STRING; 3702.AT2G26800.2; -.
DR iPTMnet; O81027; -.
DR PaxDb; O81027; -.
DR PRIDE; O81027; -.
DR EnsemblPlants; AT2G26800.1; AT2G26800.1; AT2G26800. [O81027-2]
DR EnsemblPlants; AT2G26800.2; AT2G26800.2; AT2G26800. [O81027-1]
DR EnsemblPlants; AT2G26800.4; AT2G26800.4; AT2G26800. [O81027-1]
DR GeneID; 817221; -.
DR Gramene; AT2G26800.1; AT2G26800.1; AT2G26800. [O81027-2]
DR Gramene; AT2G26800.2; AT2G26800.2; AT2G26800. [O81027-1]
DR Gramene; AT2G26800.4; AT2G26800.4; AT2G26800. [O81027-1]
DR KEGG; ath:AT2G26800; -.
DR Araport; AT2G26800; -.
DR TAIR; locus:2039548; AT2G26800.
DR eggNOG; KOG2368; Eukaryota.
DR InParanoid; O81027; -.
DR OrthoDB; 1029775at2759; -.
DR PhylomeDB; O81027; -.
DR BioCyc; ARA:AT2G26800-MON; -.
DR UniPathway; UPA00896; UER00863.
DR PRO; PR:O81027; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81027; baseline and differential.
DR Genevisible; O81027; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0046951; P:ketone body biosynthetic process; IBA:GO_Central.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; PTHR42738; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lyase; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..468
FT /note="Hydroxymethylglutaryl-CoA lyase, mitochondrial"
FT /id="PRO_0000389611"
FT DOMAIN 168..435
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT ACT_SITE 401
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 370
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_038469"
SQ SEQUENCE 468 AA; 50577 MW; C91C70DAD241AF74 CRC64;
MQWNGVRRAH SIWCKRLTNN THLHHPSIPV SHFFTMSSLE EPLSFDKLPS MSTMDRIQRF
SSGACRPRDD VGMGHRWIEG RDCTTSNSCI DDDKSFAKES FPWRRHTRKL SEGEHMFRNI
SFAGRTSTVS GTLRESKSFK EQKYSTFSNE NGTSHISNKI SKGIPKFVKI VEVGPRDGLQ
NEKNIVPTSV KVELIQRLVS SGLPVVEATS FVSPKWVPQL ADAKDVMDAV NTLDGARLPV
LTPNLKGFQA AVSAGAKEVA IFASASESFS LSNINCTIEE SLLRYRVVAT AAKEHSVPVR
GYVSCVVGCP VEGPVLPSKV AYVVKELYDM GCFEISLGDT IGIGTPGSVV PMLEAVMAVV
PADKLAVHFH DTYGQALANI LVSLQMGISI VDSSIAGLGG CPYAKGASGN VATEDVVYML
NGLGVHTNVD LGKLIAAGDF ISKHLGRPNG SKAAVALNRR ITADASKI
