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Database: UniProt
Entry: A0A498LWA2_LABRO
LinkDB: A0A498LWA2_LABRO
Original site: A0A498LWA2_LABRO 
ID   A0A498LWA2_LABRO        Unreviewed;       518 AA.
AC   A0A498LWA2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000256|ARBA:ARBA00012978, ECO:0000256|RuleBase:RU364071};
DE            Short=HMG-CoA synthase {ECO:0000256|RuleBase:RU364071};
DE            EC=2.3.3.10 {ECO:0000256|ARBA:ARBA00012978, ECO:0000256|RuleBase:RU364071};
DE   AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase {ECO:0000256|ARBA:ARBA00033130, ECO:0000256|RuleBase:RU364071};
GN   ORFNames=ROHU_010428 {ECO:0000313|EMBL:RXN11822.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN11822.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN11822.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN11822.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN11822.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) 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   -!- 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:RXN11822.1}.
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DR   EMBL; QBIY01013105; RXN11822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498LWA2; -.
DR   STRING; 84645.A0A498LWA2; -.
DR   UniPathway; UPA00058; UER00102.
DR   Proteomes; UP000290572; 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: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: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   1: Evidence at protein level;
KW   Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW   Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364071};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A498LWA2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572};
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          13..186
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          188..470
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   REGION          496..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        95
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        129
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        264
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   BINDING         221
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         269
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         273
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
SQ   SEQUENCE   518 AA;  57073 MW;  267906543B6D9ECA CRC64;
     MPGSLPTVCE AAWPKDVGII AMEVYVPSQY VDQTELEEYD GVGAGKYTVG LGQARMGFCS
     DREDINSLCL TVVQRLMERN GLSYESVGRL EVGTETIIDK SKSTKTVLMQ LFEESGNTDV
     EGVDTTNACY GGTAALFNAV NWVESSSWDG RYALVVAGDI AVYATGSARP TGGAGAVAML
     VGPNAPLAFE RGLRGTHMQH AYDFYKPDMV SEYPVVDGKL SIQCYLSALD RCYSVYRNKI
     HAQWQREGLD KRCSLEDFGF MVFHSPYCKL VQKSLARLML NDFLCHPSPN TESGPFSGLD
     SFRDVKIEET YFDRDVEKAF MKASSELFDN KTKASLLISN QNGNMYTPSV YGCLASVLAQ
     HTPQQLAGQR IGVFSYGSGF AATLYSIKVT QDATPGSALD KMVSSLCDLQ ARLDSRKKVS
     PDVFAQNMKL REETHHLANY IPQGSVDELF PGTWYLTRVD EKHRRQYARR SMNDDRPLEA
     GLVSSSIAAE HIPSPLKKMP RIPTTTAGPE VVISNGEH
//
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