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Database: UniProt
Entry: A0A421JLH8_9ASCO
LinkDB: A0A421JLH8_9ASCO
Original site: A0A421JLH8_9ASCO 
ID   A0A421JLH8_9ASCO        Unreviewed;       447 AA.
AC   A0A421JLH8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
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};
GN   ORFNames=JA1_003777 {ECO:0000313|EMBL:RLV91546.1};
OS   Spathaspora sp. JA1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV91546.1, ECO:0000313|Proteomes:UP000285775};
RN   [1] {ECO:0000313|EMBL:RLV91546.1, ECO:0000313|Proteomes:UP000285775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA1 {ECO:0000313|EMBL:RLV91546.1,
RC   ECO:0000313|Proteomes:UP000285775};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) 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|RuleBase:RU364071};
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC       family. {ECO:0000256|ARBA:ARBA00007061, ECO:0000256|RuleBase:RU364071}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV91546.1}.
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DR   EMBL; NSGQ01000034; RLV91546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JLH8; -.
DR   STRING; 2028339.A0A421JLH8; -.
DR   Proteomes; UP000285775; Unassembled WGS sequence.
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: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:SF2; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364071}.
FT   DOMAIN          4..173
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          174..446
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   ACT_SITE        84
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        116
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        246
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   BINDING         207
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         251
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         255
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
SQ   SEQUENCE   447 AA;  49733 MW;  270221738792B648 CRC64;
     MTQQKIGIKA IEVYIPGQAV NQTDLEKFDN IPAGKYTIGL GQTNMAFVND REDIYSISLT
     VLSKLINNYN IDTDKIGRLE VGTETLLDKS KSVKSVLMQL FPDNNDIEGI DTVNACYGGT
     SAIINAINWL ESSSWDGRDA IVVAGDIAIY DKGAARPTGG CGAIALLIGP DAPIVFDPIR
     GSFMEHAYDF YKPDFTSEYP VVDGHFSLAC YVKAVDQCYR NYSKKYTKDS GKTVGVFDHF
     DYNAFHVPTC KLVTKSYARL LYNDYLSNPE KFVDLIPEET RKTIDGLTYE QSLIDKTWEK
     TFVALAKEET KSRVQPALQV PTNTGNMYTA SAWVSLASLL YYVGSENVQD KRIGVFSYGS
     GLAATLLSVR VVGDISKITK VLDFDYKLGE GRKIESPEQF VAAIELREAA HLQKSFVPTG
     SIENLAQGTY YLQEIDEKFR RKYAIKN
//
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