ID H3DHM2_TETNG Unreviewed; 330 AA.
AC H3DHM2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Hydroxymethylglutaryl-CoA lyase, mitochondrial {ECO:0000256|ARBA:ARBA00014045};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
DE AltName: Full=3-hydroxy-3-methylglutarate-CoA lyase {ECO:0000256|ARBA:ARBA00030891};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000020016.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000020016.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that
CC catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-
CC methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in
CC ketogenesis. Terminal step in leucine catabolism. Ketone bodies (beta-
CC hydroxybutyrate, acetoacetate and acetone) are essential as an
CC alternative source of energy to glucose, as lipid precursors and as
CC regulators of metabolism. {ECO:0000256|ARBA:ARBA00002768}.
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 -!- SUBUNIT: Homodimer; disulfide-linked. Can also form homotetramers.
CC {ECO:0000256|ARBA:ARBA00011413}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC {ECO:0000256|ARBA:ARBA00009405}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H3DHM2; -.
DR STRING; 99883.ENSTNIP00000020016; -.
DR Ensembl; ENSTNIT00000020247.1; ENSTNIP00000020016.1; ENSTNIG00000016898.1.
DR GeneTree; ENSGT00940000158484; -.
DR InParanoid; H3DHM2; -.
DR OMA; FQMRNTH; -.
DR TreeFam; TF105363; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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:SF1; HYDROXYMETHYLGLUTARYL-COA LYASE, MITOCHONDRIAL; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303}.
FT DOMAIN 38..305
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 330 AA; 34920 MW; 315C725A7779094F CRC64;
MCQQYLAFSS AGKSAPLVWV TRSRTAGLRA CQTLPEKVKI VEVGPRDGLQ NEKTIVPSET
KIHLIDLLSA SGLPVIEATS FVSPKWVPQM ADQVEVMKGI SRRPGVSYPV LTPNLKGFQA
AVQAGASEVA IFGAASELFS KKNINCSVDE SLQRFDEVMK AAKEAGVPVR GYVSCVLGCP
YEGKVEPVKV AHVAKRLYAM GCYEISLGDT IGVGTPGSMR DMLEVVSREV PVSALAVHCH
DTYGQALANI LVALQMGVSV VDSSVAGLGG CPYAQGASGN VATEDVVYML HGLGIQTGVD
LSKVMDAGAF ICRSLNRRTN SKVAQATCKL
//
