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Database: UniProt
Entry: S2KGM2_MUCC1
LinkDB: S2KGM2_MUCC1
Original site: S2KGM2_MUCC1 
ID   S2KGM2_MUCC1            Unreviewed;       452 AA.
AC   S2KGM2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=HMPREF1544_01681 {ECO:0000313|EMBL:EPB91550.1};
OS   Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS   agent) (Calyptromyces circinelloides).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB91550.1, ECO:0000313|Proteomes:UP000014254};
RN   [1] {ECO:0000313|Proteomes:UP000014254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL   Submitted (MAY-2013) 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}.
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DR   EMBL; KE123908; EPB91550.1; -; Genomic_DNA.
DR   AlphaFoldDB; S2KGM2; -.
DR   STRING; 1220926.S2KGM2; -.
DR   VEuPathDB; FungiDB:HMPREF1544_01681; -.
DR   eggNOG; KOG1393; Eukaryota.
DR   InParanoid; S2KGM2; -.
DR   OMA; DDAYNWI; -.
DR   OrthoDB; 1060at2759; -.
DR   Proteomes; UP000014254; 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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364071}.
FT   DOMAIN          9..182
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          183..451
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   ACT_SITE        91
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        125
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        256
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   BINDING         217
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         261
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         265
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
SQ   SEQUENCE   452 AA;  50497 MW;  490B67FC9E403F67 CRC64;
     MTVPNYSNYP ENVGVLAMEM YFPKRCVIQS EMETFDGVSA GKYTIGLGQD KMAFIDDRED
     IQSICLTAVQ NLMEKHNISY SDIGRLEVGT ETIIDKSKAV KTCLMTLFTE QGNTEVEGID
     TTNACYGGFA AFSNAVNWIE SSSWDGRYAI VVAGDLALYA SGAARPTSGA GVVAMLIGKD
     APIVVERGLR STHMEHAYDF YKPDMHSEYP VVDGKFSNTC YLRAFDSCYR RYMARLAKLE
     NKEKPSLDDI DYVVCHSPYA KLVNKSFARA SYNDFLLDTD NEKFAALKPF EEMSYADSLE
     NKDLERALMG LSKAGYAQKV GPAAYAPKQI GNMYTAAVWA GLASLISEVD SETLQDKRIM
     LYSYGSGLAA SMISFRVRGS TNEIKSKLNL RERLDARTHS KPEEFAAAMK MRENTHNACN
     FNPSGSLDNI ATGVYYVEKI DDKWRRFYKR KD
//
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