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Protein

Hydroxymethylglutaryl-CoA synthase B

Gene

hgsB

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.By similarity

Catalytic activityi

Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.

Pathway:i(R)-mevalonate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Hydroxymethylglutaryl-CoA synthase A (hgsA), Hydroxymethylglutaryl-CoA synthase B (hgsB)
  3. 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1 (hmgA), 3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 (hmgB)
This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Proton donor/acceptorBy similarity
Active sitei119 – 1191Acyl-thioester intermediateBy similarity
Active sitei250 – 2501Proton donor/acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Enzyme and pathway databases

ReactomeiREACT_344579. Synthesis of Ketone Bodies.
REACT_345831. Cholesterol biosynthesis.
UniPathwayiUPA00058; UER00102.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxymethylglutaryl-CoA synthase B (EC:2.3.3.10)
Short name:
HMG-CoA synthase B
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase B
Gene namesi
Name:hgsB
ORF Names:DDB_G0274871
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195 Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0274871. hgsB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 468468Hydroxymethylglutaryl-CoA synthase BPRO_0000340242Add
BLAST

Proteomic databases

PRIDEiQ86HL5.

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0217522.

Structurei

3D structure databases

ProteinModelPortaliQ86HL5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi371 – 38414Poly-AsnAdd
BLAST

Sequence similaritiesi

Belongs to the HMG-CoA synthase family.Curated

Phylogenomic databases

eggNOGiCOG3425.
InParanoidiQ86HL5.
KOiK01641.
OMAiKLQSRHE.
PhylomeDBiQ86HL5.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

Q86HL5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTKDIGIC AIDIYFPQTY VNQSELKKYD KVSNGKYTIG LGQTNMSFVG
60 70 80 90 100
DREDIVSMAM TSVKMMMSKY SIDYQSIGRL EVGTETIIDK SKSVKSSIMS
110 120 130 140 150
LFQEYGNTSL EGVDTLNACY GGTNALFNSL QWIESSYWDG RYALVVTGDI
160 170 180 190 200
AVYSKGAARP TGGAGVVTML IGPNATLIFD QSLRGTHMEN VNDFYKPDLS
210 220 230 240 250
SEYPYVDGKL SIECYLRALD KCYLEYKKKF ESINDDNKFS MDSFDYVCFH
260 270 280 290 300
SPYNRLVQKS YARLIYNDFL QNPNNPKYQD LLPFKDLSTG KDSYINSKLD
310 320 330 340 350
QITLKLSLDD FKTKVNPSTL LSKECGNSYC GSVYSGILSL LSNVNDLNNK
360 370 380 390 400
KVLVFSYGSG LAASLFSFRI NNNKNRNNNN NNNNCFFKTT NDIGKISNIK
410 420 430 440 450
ERLSNRVKVS PEEFTRILDI REKSHQMVGA RTPIDTLDYI SAGTFYLEKI
460
DEKLIRHYKS KPIISSKL
Length:468
Mass (Da):52,921
Last modified:June 1, 2003 - v1
Checksum:iD44CCE967EF23BC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000012 Genomic DNA. Translation: EAL70328.1.
RefSeqiXP_644076.1. XM_638984.1.

Genome annotation databases

EnsemblProtistsiDDB0217522; DDB0217522; DDB_G0274871.
GeneIDi8619505.
KEGGiddi:DDB_G0274871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000012 Genomic DNA. Translation: EAL70328.1.
RefSeqiXP_644076.1. XM_638984.1.

3D structure databases

ProteinModelPortaliQ86HL5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0217522.

Proteomic databases

PRIDEiQ86HL5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0217522; DDB0217522; DDB_G0274871.
GeneIDi8619505.
KEGGiddi:DDB_G0274871.

Organism-specific databases

dictyBaseiDDB_G0274871. hgsB.

Phylogenomic databases

eggNOGiCOG3425.
InParanoidiQ86HL5.
KOiK01641.
OMAiKLQSRHE.
PhylomeDBiQ86HL5.

Enzyme and pathway databases

UniPathwayiUPA00058; UER00102.
ReactomeiREACT_344579. Synthesis of Ketone Bodies.
REACT_345831. Cholesterol biosynthesis.

Miscellaneous databases

PROiQ86HL5.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  2. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.

Entry informationi

Entry nameiHMCSB_DICDI
AccessioniPrimary (citable) accession number: Q86HL5
Secondary accession number(s): Q555J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.