GenomeNet

Database: UniProt
Entry: A0A093GHT0_DRYPU
LinkDB: A0A093GHT0_DRYPU
Original site: A0A093GHT0_DRYPU 
ID   A0A093GHT0_DRYPU        Unreviewed;       525 AA.
AC   A0A093GHT0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000256|RuleBase:RU364071};
DE            Short=HMG-CoA synthase {ECO:0000256|RuleBase:RU364071};
DE            EC=2.3.3.10 {ECO:0000256|RuleBase:RU364071};
DE   AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase {ECO:0000256|RuleBase:RU364071};
DE   Flags: Fragment;
GN   ORFNames=N307_15298 {ECO:0000313|EMBL:KFV66532.1};
OS   Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX   NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV66532.1, ECO:0000313|Proteomes:UP000053875};
RN   [1] {ECO:0000313|EMBL:KFV66532.1, ECO:0000313|Proteomes:UP000053875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV66532.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA
CC       to form HMG-CoA. {ECO:0000256|RuleBase:RU364071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-
CC         methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001222};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001222};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00005218, ECO:0000256|RuleBase:RU364071}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC       family. {ECO:0000256|ARBA:ARBA00007061, ECO:0000256|RuleBase:RU364071}.
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; KL215784; KFV66532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093GHT0; -.
DR   STRING; 118200.A0A093GHT0; -.
DR   UniPathway; UPA00058; UER00102.
DR   Proteomes; UP000053875; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR   CDD; cd00827; init_cond_enzymes; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR000590; HMG_CoA_synt_AS.
DR   InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR   InterPro; IPR013528; HMG_CoA_synth_N.
DR   InterPro; IPR010122; HMG_CoA_synthase_euk.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR01833; HMG-CoA-S_euk; 1.
DR   PANTHER; PTHR43323; 3-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASE; 1.
DR   PANTHER; PTHR43323:SF4; HYDROXYMETHYLGLUTARYL-COA SYNTHASE, CYTOPLASMIC; 1.
DR   Pfam; PF08540; HMG_CoA_synt_C; 1.
DR   Pfam; PF01154; HMG_CoA_synt_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS01226; HMG_COA_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU364071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053875};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955,
KW   ECO:0000256|RuleBase:RU364071};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW   ECO:0000256|RuleBase:RU364071};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011,
KW   ECO:0000256|RuleBase:RU364071};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166,
KW   ECO:0000256|RuleBase:RU364071};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364071}.
FT   DOMAIN          16..189
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          190..473
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   ACT_SITE        98
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        132
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        267
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   BINDING         170
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         224
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         272
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         276
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV66532.1"
FT   NON_TER         525
FT                   /evidence="ECO:0000313|EMBL:KFV66532.1"
SQ   SEQUENCE   525 AA;  57894 MW;  E14C2029E7CF377C CRC64;
     STTMPGSLPV NAESCWPKDV GIVALEIYFP SQYVDQTELE KYDGVDAGKY TIGLGQSRMG
     FCSDREDINS LCLTVVQKLM ERNSLSYDCI GRLEVGTETI IDKSKSVKTV LMQLFEESGN
     TDVEGIDTTN ACYGGTAALF NAINWIESSS WDGRYALVVA GDIAVYASGN ARPTGGAGAV
     AMLVGPNAPL IFERGLRGTH MQHAYDFYKP DMVSEYPVVD GKLSIQCYLS ALDRCYTVYR
     NKIQAQWQKE GIDRCFTLND FGFMIFHSPY CKLVQKSVAR LLLNDFLSDQ NPETANGVFS
     GLEAFRDIKL EDTYFDRDVE KAFMKASAEL FNQKTKASLL VSNQNGNMYT PSVYGCLASL
     LAQYSPEQLA GQRISVFSYG SGFAATLYSI RVTQDATPGS ALDKITASLS DLKARLDSRK
     CIAPDVFAEN MKIRQETHHL ANYIPQCSVE DLFDGTWYLV RVDEKHRRTY ARRPVMGDGP
     LEAGVEAVHP GIVHEHIPSP AKKVPRIPAT TESEGVTVAI SNGEH
//
DBGET integrated database retrieval system