ID A0A067F220_CITSI Unreviewed; 354 AA.
AC A0A067F220;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=CISIN_1g012253mg {ECO:0000313|EMBL:KDO60145.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO60145.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO60145.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
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|RuleBase:RU364071};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC {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; KK784934; KDO60145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067F220; -.
DR UniPathway; UPA00058; UER00102.
DR Proteomes; UP000027120; 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 GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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 Lipid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW Lipid metabolism {ECO:0000256|RuleBase:RU364071};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW Steroid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW Steroid metabolism {ECO:0000256|RuleBase:RU364071};
KW Sterol biosynthesis {ECO:0000256|RuleBase:RU364071};
KW Sterol metabolism {ECO:0000256|RuleBase:RU364071};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364071}.
FT DOMAIN 6..178
FT /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01154"
FT DOMAIN 179..350
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT ACT_SITE 121
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT ACT_SITE 251
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT BINDING 213
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT BINDING 256
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT BINDING 260
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
SQ SEQUENCE 354 AA; 39194 MW; 435C665EE65E07E3 CRC64;
MTSWHPKNVG ILALDIYFPP TCVLQEALEV HDGVSKGKYT VGLGQDCMAF CSEVEDVISM
SLTVVTSLLE KYKIDPTQIG RLEVGSETVI DKSKSIKTFL MQIFEKYGNT DIEGVDSTNA
CYGGTAALFN CVNWVESASW DGRYGLVVCT DSAVYAEGPA RPTGGAAAVA MLIGPDAPIA
FESKLRGSHM SHAYDFYKPN LASEYPVVDG KLSQTCYLMA LDSCYKYFCQ KFEKLEGRQF
SMLDVDYFVF HSPYNKLVQK SFARLFFNDF LRNASSVDEI AKEKLAPYST LSDVESYQSR
DLEKASQQVA KQLYDLKVQP STLIPKQVGN MYTASLYAAF ASLLHEKHSS LVSG
//
