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Q9HGZ6

- FDFT_CANGA

UniProt

Q9HGZ6 - FDFT_CANGA

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Protein

Squalene synthase

Gene

ERG9

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

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 activityi

2 farnesyl diphosphate + NAD(P)H = squalene + 2 diphosphate + NAD(P)+.

Cofactori

Magnesium.By similarity

Pathwayi

GO - Molecular functioni

  1. farnesyl-diphosphate farnesyltransferase activity Source: CGD
  2. oxidoreductase activity Source: UniProtKB-KW
  3. squalene synthase activity Source: CGD

GO - Biological processi

  1. ergosterol biosynthetic process Source: CGD
  2. isoprenoid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

Magnesium, NADP

Enzyme and pathway databases

UniPathwayiUPA00767; UER00751.

Names & Taxonomyi

Protein namesi
Recommended name:
Squalene synthase (EC:2.5.1.21)
Short name:
SQS
Short name:
SS
Alternative name(s):
FPP:FPP farnesyltransferase
Farnesyl-diphosphate farnesyltransferase
Gene namesi
Name:ERG9
Ordered Locus Names:CAGL0M07095g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428: Chromosome M

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Squalene synthasePRO_0000067448Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9HGZ6.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei181 – 20121HelicalSequence AnalysisAdd
BLAST
Transmembranei294 – 31421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the phytoene/squalene synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000186940.
InParanoidiQ9HGZ6.
KOiK00801.
OMAiEMRHAVC.
OrthoDBiEOG7GJ6P5.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamiPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
TIGRFAMsiTIGR01559. squal_synth. 1 hit.
PROSITEiPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HGZ6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKVLDLALH PLELRAALKL KFIRQPLFST NDTRATPQLE RCYELLNLTS
60 70 80 90 100
RSFAAVIMEL HPELRNVIMV FYLILRALDT VEDDMTIDPQ LKVKVLREFD
110 120 130 140 150
SKLDTTDWSF DGNDLKEKDR VVLTEFPCIL GEYHKLKPEY QKVIKRITGL
160 170 180 190 200
MGNGMADYIL DENFNLNGVQ TVKDYDKYCH YVAGLVGDGL TELIVLAGFG
210 220 230 240 250
SDDLYHGKNS FQLYESMGLF LQKTNIIRDY AEDLDDGRSF WPKEIWSEYA
260 270 280 290 300
TKLTDFRDPK NTQKGVDCIN HLVLNALTHV IDVLTYLSSI HEQSSFQFCA
310 320 330 340 350
IPQVMAIATL AKVFNNPEVL RKNVKIRKGT TCDLILNSRT LKGCVDIFQY
360 370 380 390 400
YLRDMKQRLP VEDPNYLKFN IQVAKIEQFI EEMFQDNLPA GVEPRETMIY
410 420 430 440
LKVQERLKWD TQVIPRVQEE DYKFNMALSV VFCVLLSFYF FTK
Length:443
Mass (Da):51,397
Last modified:August 31, 2004 - v2
Checksum:iC23BC9D603E44C9F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171M → L in BAB12207. (PubMed:10952588)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB009978 Genomic DNA. Translation: BAB12207.1.
CR380959 Genomic DNA. Translation: CAG62632.1.
RefSeqiXP_449656.1. XM_449656.1.

Genome annotation databases

GeneIDi2891705.
KEGGicgr:CAGL0M07095g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB009978 Genomic DNA. Translation: BAB12207.1 .
CR380959 Genomic DNA. Translation: CAG62632.1 .
RefSeqi XP_449656.1. XM_449656.1.

3D structure databases

ProteinModelPortali Q9HGZ6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2891705.
KEGGi cgr:CAGL0M07095g.

Phylogenomic databases

HOGENOMi HOG000186940.
InParanoidi Q9HGZ6.
KOi K00801.
OMAi EMRHAVC.
OrthoDBi EOG7GJ6P5.

Enzyme and pathway databases

UniPathwayi UPA00767 ; UER00751 .

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
InterProi IPR002060. Squ/phyt_synthse.
IPR006449. Squal_synth.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF00494. SQS_PSY. 1 hit.
[Graphical view ]
SUPFAMi SSF48576. SSF48576. 1 hit.
TIGRFAMsi TIGR01559. squal_synth. 1 hit.
PROSITEi PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., 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.

Entry informationi

Entry nameiFDFT_CANGA
AccessioniPrimary (citable) accession number: Q9HGZ6
Secondary accession number(s): Q6FJD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: August 31, 2004
Last modified: October 29, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3