Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei41Farnesyl diphosphate 11
Binding sitei168Farnesyl diphosphate 21
Binding sitei171Farnesyl diphosphate 11
Binding sitei172Farnesyl diphosphate 21
Binding sitei248Farnesyl diphosphate 11

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 databases

ChEMBLiCHEMBL5440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003473351 – 287Dehydrosqualene synthaseAdd BLAST287

Interactioni

Protein-protein interaction databases

STRINGi93062.SACOL2577.

Chemistry databases

BindingDBiA9JQL9.

Structurei

Secondary structure

1287
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Helixi20 – 26Combined sources7
Helixi31 – 49Combined sources19
Helixi50 – 53Combined sources4
Beta strandi55 – 57Combined sources3
Helixi58 – 72Combined sources15
Helixi84 – 96Combined sources13
Helixi101 – 114Combined sources14
Helixi123 – 133Combined sources11
Helixi135 – 145Combined sources11
Helixi151 – 171Combined sources21
Helixi173 – 178Combined sources6
Helixi186 – 192Combined sources7
Helixi196 – 202Combined sources7
Helixi206 – 228Combined sources23
Helixi229 – 232Combined sources4
Helixi237 – 257Combined sources21
Turni258 – 260Combined sources3
Beta strandi262 – 264Combined sources3
Helixi270 – 283Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA9JQL9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 22Farnesyl diphosphate 1 binding5
Regioni45 – 48Farnesyl diphosphate 2 binding4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105FE1. Bacteria.
COG1562. LUCA.

Family and domain databases

CDDicd00683. Trans_IPPS_HH. 1 hit.
Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR002060. Squ/phyt_synthse.
IPR019845. Squalene/phytoene_synthase_CS.
IPR033904. Trans_IPPS_HH.
[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_LWRD01000002.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920687 Genomic DNA. Translation: CAP47341.1.
RefSeqiWP_000178319.1. NZ_LWRD01000002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93062.SACOL2577.

Chemistry databases

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

CDDicd00683. Trans_IPPS_HH. 1 hit.
Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR002060. Squ/phyt_synthse.
IPR019845. Squalene/phytoene_synthase_CS.
IPR033904. Trans_IPPS_HH.
[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: November 30, 2016
This is version 45 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.