Squalene synthase - Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast)

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Q9HGZ6 (FDFT_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Squalene synthase
Short name=SQS
Short name=SS
EC=2.5.1.21

Alternative name(s):
FPP:FPP farnesyltransferase
Farnesyl-diphosphate farnesyltransferase

Gene names

Name:	ERG9
Ordered Locus Names:	CAGL0M07095g

Organism

Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

284593 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces ›

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation of 2 two farnesyl pyrophosphate moieties to form squalene. It is the first committed enzyme of the sterol biosynthesis pathway. Required for the biosynthesis of ergosterol.
Catalytic activity	2 farnesyl diphosphate + NAD(P)H = squalene + 2 diphosphate + NAD(P)⁺.
Cofactor	Magnesium By similarity.
Pathway	Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 1/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the phytoene/squalene synthase family.

Ontologies

Keywords
Biological process	Isoprene biosynthesis Lipid biosynthesis Lipid metabolism Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Magnesium NADP
Molecular function	Oxidoreductase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW sterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	farnesyl-diphosphate farnesyltransferase activity Inferred from electronic annotation. Source: EC oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW squalene 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 – 443

443

Squalene synthase

PRO_0000067448

Regions

Transmembrane

181 – 201

Helical; Potential

Transmembrane

294 – 314

Helical; Potential

Experimental info

Sequence conflict

217

M → L in BAB12207. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9HGZ6 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: C23BC9D603E44C9F
Show »

FASTA

443

51,397

        10         20         30         40         50         60 
MGKVLDLALH PLELRAALKL KFIRQPLFST NDTRATPQLE RCYELLNLTS RSFAAVIMEL 

        70         80         90        100        110        120 
HPELRNVIMV FYLILRALDT VEDDMTIDPQ LKVKVLREFD SKLDTTDWSF DGNDLKEKDR 

       130        140        150        160        170        180 
VVLTEFPCIL GEYHKLKPEY QKVIKRITGL MGNGMADYIL DENFNLNGVQ TVKDYDKYCH 

       190        200        210        220        230        240 
YVAGLVGDGL TELIVLAGFG SDDLYHGKNS FQLYESMGLF LQKTNIIRDY AEDLDDGRSF 

       250        260        270        280        290        300 
WPKEIWSEYA TKLTDFRDPK NTQKGVDCIN HLVLNALTHV IDVLTYLSSI HEQSSFQFCA 

       310        320        330        340        350        360 
IPQVMAIATL AKVFNNPEVL RKNVKIRKGT TCDLILNSRT LKGCVDIFQY YLRDMKQRLP 

       370        380        390        400        410        420 
VEDPNYLKFN IQVAKIEQFI EEMFQDNLPA GVEPRETMIY LKVQERLKWD TQVIPRVQEE 

       430        440 
DYKFNMALSV VFCVLLSFYF FTK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Depletion of the squalene synthase (ERG9) gene does not impair growth of Candida glabrata in mice." Nakayama H., Izuta M., Nakayama N., Arisawa M., Aoki Y. Antimicrob. Agents Chemother. 44:2411-2418(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L. Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB009978 Genomic DNA. Translation: BAB12207.1. CR380959 Genomic DNA. Translation: CAG62632.1.
RefSeq	XP_449656.1. XM_449656.1.
3D structure databases
ProteinModelPortal	Q9HGZ6.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2891705.
KEGG	cgr:CAGL0M07095g.
Phylogenomic databases
HOGENOM	HOG000186940.
KO	K00801.
OMA	ELRHAVC.
OrthoDB	EOG4BP4MQ.
Enzyme and pathway databases
UniPathway	UPA00767; UER00751.
Family and domain databases
Gene3D	1.10.600.10. 1 hit.
InterPro	IPR002060. Squ/phyt_synthse. IPR006449. Squal_synth. IPR019845. Squalene/phytoene_synthase_CS. IPR008949. Terpenoid_synth. [Graphical view]
Pfam	PF00494. SQS_PSY. 1 hit. [Graphical view]
SUPFAM	SSF48576. Terpenoid_synth. 1 hit.
TIGRFAMs	TIGR01559. squal_synth. 1 hit.
PROSITE	PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit. PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FDFT_CANGA

Accession

Primary (citable) accession number: Q9HGZ6
Secondary accession number(s): Q6FJD8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	August 31, 2004
Last modified:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents