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Protein

Dehydrosqualene synthase

Gene

crtM

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid dehydrosqualene (4,4'-diapophytoene). This is the initial step in the biosynthesis of staphyloxanthin, an orange carotenoid present in most staphylococci strains.1 Publication

Catalytic activityi

2 (2E,6E)-farnesyl diphosphate = 15-cis-4,4'-diapophytoene + 2 diphosphate.1 Publication

Pathwayi: staphyloxanthin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes staphyloxanthin from farnesyl diphosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Dehydrosqualene synthase (crtM)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway staphyloxanthin biosynthesis, which is itself part of Carotenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes staphyloxanthin from farnesyl diphosphate, the pathway staphyloxanthin biosynthesis and in Carotenoid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411Farnesyl diphosphate 1
Binding sitei168 – 1681Farnesyl diphosphate 2
Binding sitei171 – 1711Farnesyl diphosphate 1
Binding sitei172 – 1721Farnesyl diphosphate 2
Binding sitei248 – 2481Farnesyl diphosphate 1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Carotenoid biosynthesis

Enzyme and pathway databases

BRENDAi2.5.1.96. 3352.
UniPathwayiUPA00029; UER00556.

Names & Taxonomyi

Protein namesi
Recommended name:
Dehydrosqualene synthase (EC:2.5.1.961 Publication)
Alternative name(s):
4,4'-diapophytoene synthase
Short name:
DAP synthase
Diapophytoene synthase
Gene namesi
Name:crtM
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 287287Dehydrosqualene synthasePRO_0000347335Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL2577.

Chemistry

BindingDBiA9JQL9.

Structurei

Secondary structure

1
287
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816Combined sources
Helixi20 – 267Combined sources
Helixi31 – 4919Combined sources
Helixi50 – 534Combined sources
Beta strandi55 – 573Combined sources
Helixi58 – 7215Combined sources
Helixi84 – 9613Combined sources
Helixi101 – 11414Combined sources
Helixi123 – 13311Combined sources
Helixi135 – 14511Combined sources
Helixi151 – 17121Combined sources
Helixi173 – 1786Combined sources
Helixi186 – 1927Combined sources
Helixi196 – 2027Combined sources
Helixi206 – 22823Combined sources
Helixi229 – 2324Combined sources
Helixi237 – 25721Combined sources
Turni258 – 2603Combined sources
Beta strandi262 – 2643Combined sources
Helixi270 – 28314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZCOX-ray1.58A1-287[»]
2ZCQX-ray2.38A1-287[»]
2ZCRX-ray1.92A1-287[»]
2ZCSX-ray2.03A1-287[»]
2ZY1X-ray1.78A1-287[»]
3ACWX-ray1.63A1-287[»]
3ACXX-ray1.31A1-287[»]
3ACYX-ray1.84A1-287[»]
3ADZX-ray1.89A1-287[»]
3AE0X-ray2.37A/B1-287[»]
3LGZX-ray2.41B1-287[»]
3NPRX-ray2.00A1-287[»]
3TFNX-ray2.07A1-287[»]
3TFPX-ray2.00A1-287[»]
3TFVX-ray3.00A1-287[»]
3VJDX-ray1.48A1-287[»]
3VJEX-ray2.12A/B1-287[»]
3W7FX-ray2.25A/B1-287[»]
4E9UX-ray2.10A1-287[»]
4E9ZX-ray2.06A1-287[»]
4EA0X-ray2.12A/B1-287[»]
4EA1X-ray2.46A1-287[»]
4EA2X-ray2.05A1-287[»]
4F6VX-ray2.30A1-287[»]
4F6XX-ray1.98A1-287[»]
ProteinModelPortaliA9JQL9.
SMRiA9JQL9. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA9JQL9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 225Farnesyl diphosphate 1 binding
Regioni45 – 484Farnesyl diphosphate 2 binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105FE1. Bacteria.
COG1562. LUCA.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR002060. Squ/phyt_synthse.
IPR019845. Squalene/phytoene_synthase_CS.
[Graphical view]
PfamiPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9JQL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTMMDMNFKY CHKIMKKHSK SFSYAFDLLP EDQRKAVWAI YAVCRKIDDS
60 70 80 90 100
IDVYGDIQFL NQIKEDIQSI EKYPYEYHHF QSDRRIMMAL QHVAQHKNIA
110 120 130 140 150
FQSFYNLIDT VYKDQHFTMF ETDAELFGYC YGVAGTVGEV LTPILSDHET
160 170 180 190 200
HQTYDVARRL GESLQLINIL RDVGEDFENE RIYFSKQRLK QYEVDIAEVY
210 220 230 240 250
QNGVNNHYID LWEYYAAIAE KDFRDVMDQI KVFSIEAQPI IELAARIYIE
260 270 280
ILDEVRQANY TLHERVFVEK RKKAKLFHEI NSKYHRI
Length:287
Mass (Da):34,313
Last modified:February 5, 2008 - v1
Checksum:i41AD734ABEB81214
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920687 Genomic DNA. Translation: CAP47341.1.
RefSeqiWP_000178319.1. NZ_LN626917.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920687 Genomic DNA. Translation: CAP47341.1.
RefSeqiWP_000178319.1. NZ_LN626917.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZCOX-ray1.58A1-287[»]
2ZCQX-ray2.38A1-287[»]
2ZCRX-ray1.92A1-287[»]
2ZCSX-ray2.03A1-287[»]
2ZY1X-ray1.78A1-287[»]
3ACWX-ray1.63A1-287[»]
3ACXX-ray1.31A1-287[»]
3ACYX-ray1.84A1-287[»]
3ADZX-ray1.89A1-287[»]
3AE0X-ray2.37A/B1-287[»]
3LGZX-ray2.41B1-287[»]
3NPRX-ray2.00A1-287[»]
3TFNX-ray2.07A1-287[»]
3TFPX-ray2.00A1-287[»]
3TFVX-ray3.00A1-287[»]
3VJDX-ray1.48A1-287[»]
3VJEX-ray2.12A/B1-287[»]
3W7FX-ray2.25A/B1-287[»]
4E9UX-ray2.10A1-287[»]
4E9ZX-ray2.06A1-287[»]
4EA0X-ray2.12A/B1-287[»]
4EA1X-ray2.46A1-287[»]
4EA2X-ray2.05A1-287[»]
4F6VX-ray2.30A1-287[»]
4F6XX-ray1.98A1-287[»]
ProteinModelPortaliA9JQL9.
SMRiA9JQL9. Positions 1-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL2577.

Chemistry

BindingDBiA9JQL9.
ChEMBLiCHEMBL5440.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105FE1. Bacteria.
COG1562. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00029; UER00556.
BRENDAi2.5.1.96. 3352.

Miscellaneous databases

EvolutionaryTraceiA9JQL9.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR002060. Squ/phyt_synthse.
IPR019845. Squalene/phytoene_synthase_CS.
[Graphical view]
PfamiPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCRTM_STAAU
AccessioniPrimary (citable) accession number: A9JQL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 5, 2008
Last modified: March 16, 2016
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.