HMCS_ARATH
ID HMCS_ARATH Reviewed; 461 AA.
AC P54873; Q8L721; Q9S707;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Hydroxymethylglutaryl-CoA synthase;
DE Short=HMG-CoA synthase;
DE EC=2.3.3.10;
DE AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2778;
DE AltName: Full=Protein FLAKY POLLEN 1;
GN Name=HMGS; Synonyms=EMB2778, FKP1, MVA1; OrderedLocusNames=At4g11820;
GN ORFNames=T26M18.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8566777; DOI=10.1016/0378-1119(95)00642-7;
RA Montamat F., Guilloton M., Karst F., Delrot S.;
RT "Isolation and characterization of a cDNA encoding Arabidopsis thaliana 3-
RT hydroxy-3-methylglutaryl-coenzyme A synthase.";
RL Gene 167:197-201(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Connolly E.L., Learned R.M.;
RT "Post-transcriptional regulation of HMG-CoA synthase expression in
RT Arabidopsis thaliana.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20484369; DOI=10.1093/pcp/pcq068;
RA Ishiguro S., Nishimori Y., Yamada M., Saito H., Suzuki T., Nakagawa T.,
RA Miyake H., Okada K., Nakamura K.;
RT "The Arabidopsis FLAKY POLLEN1 gene encodes a 3-hydroxy-3-methylglutaryl-
RT coenzyme A synthase required for development of tapetum-specific organelles
RT and fertility of pollen grains.";
RL Plant Cell Physiol. 51:896-911(2010).
CC -!- FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form
CC HMG-CoA, which is the substrate for HMG-CoA reductase. Devoided of
CC acetoacetyl-CoA thiolase (AACT) activity. Required for the development
CC of both tapetosomes and elaioplasts in tapetal cells and for pollen
CC viability during pollen tube elongation. {ECO:0000269|PubMed:20484369}.
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:0000255|PROSITE-ProRule:PRU10116,
CC ECO:0000269|PubMed:8566777};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P54873-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P54873-2; Sequence=VSP_008902;
CC -!- TISSUE SPECIFICITY: Highly expressed in flower buds, pollen grains and
CC anthers in the tapetal cells, at an intermediate levels in roots and
CC weakly in leaves. {ECO:0000269|PubMed:20484369}.
CC -!- DISRUPTION PHENOTYPE: Defect in pollen adhesion to the stigma resulting
CC in male sterility under normal growth conditions.
CC {ECO:0000269|PubMed:20484369}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000305}.
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DR EMBL; X83882; CAA58763.1; -; mRNA.
DR EMBL; U79160; AAD00297.1; -; mRNA.
DR EMBL; U79161; AAD00298.1; -; Genomic_DNA.
DR EMBL; AL078606; CAB44320.1; -; Genomic_DNA.
DR EMBL; AL161532; CAB78225.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83052.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83053.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67916.1; -; Genomic_DNA.
DR EMBL; AY140008; AAM98150.1; -; mRNA.
DR EMBL; BT008492; AAP37851.1; -; mRNA.
DR PIR; T09341; T09341.
DR RefSeq; NP_001319906.1; NM_001340735.1. [P54873-2]
DR RefSeq; NP_192919.1; NM_117251.3. [P54873-1]
DR RefSeq; NP_849361.1; NM_179030.1. [P54873-2]
DR AlphaFoldDB; P54873; -.
DR SMR; P54873; -.
DR BioGRID; 12086; 5.
DR STRING; 3702.AT4G11820.2; -.
DR PaxDb; P54873; -.
DR PRIDE; P54873; -.
DR ProteomicsDB; 230353; -. [P54873-1]
DR EnsemblPlants; AT4G11820.1; AT4G11820.1; AT4G11820. [P54873-2]
DR EnsemblPlants; AT4G11820.2; AT4G11820.2; AT4G11820. [P54873-1]
DR EnsemblPlants; AT4G11820.3; AT4G11820.3; AT4G11820. [P54873-2]
DR GeneID; 826788; -.
DR Gramene; AT4G11820.1; AT4G11820.1; AT4G11820. [P54873-2]
DR Gramene; AT4G11820.2; AT4G11820.2; AT4G11820. [P54873-1]
DR Gramene; AT4G11820.3; AT4G11820.3; AT4G11820. [P54873-2]
DR KEGG; ath:AT4G11820; -.
DR Araport; AT4G11820; -.
DR TAIR; locus:2137015; AT4G11820.
DR eggNOG; KOG1393; Eukaryota.
DR HOGENOM; CLU_008065_0_0_1; -.
DR InParanoid; P54873; -.
DR OMA; YFAFHAP; -.
DR OrthoDB; 495111at2759; -.
DR PhylomeDB; P54873; -.
DR BioCyc; ARA:AT4G11820-MON; -.
DR BioCyc; MetaCyc:AT4G11820-MON; -.
DR BRENDA; 2.3.3.10; 399.
DR UniPathway; UPA00058; UER00102.
DR PRO; PR:P54873; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P54873; baseline and differential.
DR Genevisible; P54873; AT.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; ISS:TAIR.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; TAS:TAIR.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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 Pfam; PF08540; HMG_CoA_synt_C; 1.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01833; HMG-CoA-S_euk; 1.
DR PROSITE; PS01226; HMG_COA_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..461
FT /note="Hydroxymethylglutaryl-CoA synthase"
FT /id="PRO_0000213756"
FT ACT_SITE 83
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 117
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 247
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_008902"
FT CONFLICT 306
FT /note="A -> S (in Ref. 1; CAA58763)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="K -> N (in Ref. 1; CAA58763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51094 MW; F44908369AFBC5A8 CRC64;
MAKNVGILAM DIYFPPTCVQ QEALEAHDGA SKGKYTIGLG QDCLAFCTEL EDVISMSFNA
VTSLFEKYKI DPNQIGRLEV GSETVIDKSK SIKTFLMQLF EKCGNTDVEG VDSTNACYGG
TAALLNCVNW VESNSWDGRY GLVICTDSAV YAEGPARPTG GAAAIAMLIG PDAPIVFESK
LRASHMAHVY DFYKPNLASE YPVVDGKLSQ TCYLMALDSC YKHLCNKFEK IEGKEFSIND
ADYIVFHSPY NKLVQKSFAR LLYNDFLRNA SSIDEAAKEK FTPYSSLTLD ESYQSRDLEK
VSQQIAKPFY DAKVQPTTLI PKEVGNMYTA SLYAAFASLI HKKHNDLAGK RVVMFSYGSG
STATMFSLRL NDNKPPFSIS NIASVMDVGG KLKARHEYAP EKFVETMKLM EHRYGAKDFV
TTKEGIIDLL APGTYYLKEV DSLYRRFYGK KGEDGSVANG H
