GenomeNet

Database: UniProt
Entry: E9H2A9_DAPPU
LinkDB: E9H2A9_DAPPU
Original site: E9H2A9_DAPPU 
ID   E9H2A9_DAPPU            Unreviewed;       319 AA.
AC   E9H2A9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   ORFNames=DAPPUDRAFT_307444 {ECO:0000313|EMBL:EFX74176.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX74176.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX74176.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
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   ---------------------------------------------------------------------------
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   EMBL; GL732585; EFX74176.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9H2A9; -.
DR   STRING; 6669.E9H2A9; -.
DR   EnsemblMetazoa; EFX74176; EFX74176; DAPPUDRAFT_307444.
DR   KEGG; dpx:DAPPUDRAFT_307444; -.
DR   eggNOG; KOG2368; Eukaryota.
DR   HOGENOM; CLU_022138_3_2_1; -.
DR   InParanoid; E9H2A9; -.
DR   OMA; FQMRNTH; -.
DR   UniPathway; UPA00896; UER00863.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046951; P:ketone body biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 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:UP000000305}.
FT   DOMAIN          25..292
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   319 AA;  34034 MW;  1F769719C0A163B0 CRC64;
     MFRKVLCNKP FIRCFTNTSQ NGNFVRMVEV GPRDGLQNEK QIVPTAAKIE FINKLSDAGL
     KSIESTSFVS PKWVPQMADH SEVLMGITKY PDVSYPVLTP NILGLNAAIK AGAKEVAVFG
     AASESFSKKN INCTVKESIH RFEEVVKEAK KHGIRIRGYV SCVVGCPYEG AIAPSAIAQV
     AEALFNVGCY EVSLGDTIGV GTPGSISKML TEVSKHIPVQ FLALHCHDTY GQALANILRG
     LDMGITVVDS SVGGLGGCPY AKGASGNVAS EEVVYMLHGL GMDTGIDLNK LIEAGQYMST
     TLGRPTGSKV SRAVLSKKC
//
DBGET integrated database retrieval system