Q86HL5 (HMCSB_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hydroxymethylglutaryl-CoA synthase B
Short name=HMG-CoA synthase B
EC=2.3.3.10

Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase B

Gene names

Name:	hgsB
ORF Names:	DDB_G0274871

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase By similarity.
Catalytic activity	Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
Sequence similarities	Belongs to the HMG-CoA synthase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	hydroxymethylglutaryl-CoA synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	Hydroxymethylglutaryl-CoA synthase B		PRO_0000340242
Regions
	Compositional bias	371 – 384	14	Poly-Asn

Sequences

	Sequence		Length	Mass (Da)
	Q86HL5 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D44CCE967EF23BC6	FASTA	468	52,921
	10 20 30 40 50 60 MKKTKDIGIC AIDIYFPQTY VNQSELKKYD KVSNGKYTIG LGQTNMSFVG DREDIVSMAM 70 80 90 100 110 120 TSVKMMMSKY SIDYQSIGRL EVGTETIIDK SKSVKSSIMS LFQEYGNTSL EGVDTLNACY 130 140 150 160 170 180 GGTNALFNSL QWIESSYWDG RYALVVTGDI AVYSKGAARP TGGAGVVTML IGPNATLIFD 190 200 210 220 230 240 QSLRGTHMEN VNDFYKPDLS SEYPYVDGKL SIECYLRALD KCYLEYKKKF ESINDDNKFS 250 260 270 280 290 300 MDSFDYVCFH SPYNRLVQKS YARLIYNDFL QNPNNPKYQD LLPFKDLSTG KDSYINSKLD 310 320 330 340 350 360 QITLKLSLDD FKTKVNPSTL LSKECGNSYC GSVYSGILSL LSNVNDLNNK KVLVFSYGSG 370 380 390 400 410 420 LAASLFSFRI NNNKNRNNNN NNNNCFFKTT NDIGKISNIK ERLSNRVKVS PEEFTRILDI 430 440 450 460 REKSHQMVGA RTPIDTLDYI SAGTFYLEKI DEKLIRHYKS KPIISSKL

References

[1]

"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000012 Genomic DNA. Translation: EAL70328.1.
RefSeq	XP_644076.1. XM_638984.1.
3D structure databases
ProteinModelPortal	Q86HL5.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDBDRAFT_0217522.
Proteomic databases
PRIDE	Q86HL5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0217522; DDB0217522; DDB_G0274871.
GeneID	8619505.
KEGG	ddi:DDB_G0274871.
Organism-specific databases
dictyBase	DDB_G0274871. hgsB.
Phylogenomic databases
eggNOG	COG3425.
KO	K01641.
OMA	ESKYRAS.
ProtClustDB	CLSZ2429883.
Enzyme and pathway databases
UniPathway	UPA00058; UER00102.
Family and domain databases
Gene3D	3.40.47.10. 1 hit.
InterPro	IPR013746. HMG_CoA_synt_C. IPR013528. HMG_CoA_synth_N. IPR010122. HMG_CoA_synthase_euk. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Pfam	PF08540. HMG_CoA_synt_C. 1 hit. PF01154. HMG_CoA_synt_N. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR01833. HMG-CoA-S_euk. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HMCSB_DICDI

Accession

Primary (citable) accession number: Q86HL5
Secondary accession number(s): Q555J1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)