A9JQL9 (CRTM_STAAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dehydrosqualene synthase
EC=2.5.1.96

Alternative name(s):
4,4'-diapophytoene synthase
Short name=DAP synthase
Diapophytoene synthase

Gene names

Name:

crtM

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C30 carotenoid dehydrosqualene (4,4'-diapophytoene). This is the initial step in the biosynthesis of staphyloxanthin, an orange carotenoid present in most staphylococci strains. Ref.1
Catalytic activity	2 (2E,6E)-farnesyl diphosphate = 4,4'-diapophytoene + 2 diphosphate. Ref.1
Pathway	Carotenoid biosynthesis; staphyloxanthin biosynthesis; staphyloxanthin from farnesyl diphosphate: step 1/5.
Sequence similarities	Belongs to the phytoene/squalene synthase family. CrtM subfamily.

Ontologies

Keywords
Biological process	Carotenoid biosynthesis
Molecular function	Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	carotenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	transferase activity, transferring alkyl or aryl (other than methyl) groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 287

287

Dehydrosqualene synthase

PRO_0000347335

Regions

Region

18 – 22

5

Farnesyl diphosphate 1 binding

Region

45 – 48

4

Farnesyl diphosphate 2 binding

Sites

Binding site

41

1

Farnesyl diphosphate 1

Binding site

168

1

Farnesyl diphosphate 2

Binding site

171

1

Farnesyl diphosphate 1

Binding site

172

1

Farnesyl diphosphate 2

Binding site

248

1

Farnesyl diphosphate 1

Secondary structure

1

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287

Helix Strand Turn

Details...

Helix

3 – 18

16

Helix

20 – 26

7

Helix

31 – 49

19

Helix

50 – 53

4

Beta strand

55 – 57

3

Helix

58 – 72

15

Helix

84 – 96

13

Helix

101 – 114

14

Helix

123 – 133

11

Helix

135 – 145

11

Helix

151 – 171

21

Helix

173 – 178

6

Helix

186 – 192

7

Helix

196 – 202

7

Helix

206 – 228

23

Helix

229 – 232

4

Helix

237 – 257

21

Turn

258 – 260

3

Beta strand

262 – 264

3

Helix

270 – 283

14

Sequences

	Sequence		Length	Mass (Da)
	A9JQL9 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 41AD734ABEB81214	FASTA	287	34,313
	10 20 30 40 50 60 MTMMDMNFKY CHKIMKKHSK SFSYAFDLLP EDQRKAVWAI YAVCRKIDDS IDVYGDIQFL 70 80 90 100 110 120 NQIKEDIQSI EKYPYEYHHF QSDRRIMMAL QHVAQHKNIA FQSFYNLIDT VYKDQHFTMF 130 140 150 160 170 180 ETDAELFGYC YGVAGTVGEV LTPILSDHET HQTYDVARRL GESLQLINIL RDVGEDFENE 190 200 210 220 230 240 RIYFSKQRLK QYEVDIAEVY QNGVNNHYID LWEYYAAIAE KDFRDVMDQI KVFSIEAQPI 250 260 270 280 IELAARIYIE ILDEVRQANY TLHERVFVEK RKKAKLFHEI NSKYHRI

References

[1]

"A cholesterol biosynthesis inhibitor blocks Staphylococcus aureus virulence." Liu C.-I., Liu G.Y., Song Y., Yin F., Hensler M.E., Jeng W.-Y., Nizet V., Wang A.H.-J., Oldfield E. Science 319:1391-1394(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEXES WITH FARNESYL THIODIPHOSPHATE AND SYNTHETIC INHIBITORS. Strain: ATCC 27659 / U9N0.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AM920687 Genomic DNA. Translation: CAP47341.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZCO	X-ray	1.58	A	1-287	[»]
2ZCP	X-ray	2.25	A/B	1-287	[»]
2ZCQ	X-ray	2.38	A	1-287	[»]
2ZCR	X-ray	1.92	A	1-287	[»]
2ZCS	X-ray	2.03	A	1-287	[»]
2ZY1	X-ray	1.78	A	1-287	[»]
3ACW	X-ray	1.63	A	1-287	[»]
3ACX	X-ray	1.31	A	1-287	[»]
3ACY	X-ray	1.84	A	1-287	[»]
3ADZ	X-ray	1.89	A	1-287	[»]
3AE0	X-ray	2.37	A/B	1-287	[»]
3LGZ	X-ray	2.41	B	1-287	[»]
3TFN	X-ray	2.07	A	1-287	[»]
3TFP	X-ray	2.00	A	1-287	[»]
3TFV	X-ray	3.00	A	1-287	[»]
3VJD	X-ray	1.48	A	1-287	[»]
3VJE	X-ray	2.12	A/B	1-287	[»]
4E9U	X-ray	2.10	A	1-287	[»]
4E9Z	X-ray	2.06	A	1-287	[»]
4EA0	X-ray	2.12	A/B	1-287	[»]
4EA1	X-ray	2.46	A	1-287	[»]
4EA2	X-ray	2.05	A	1-287	[»]
4F6V	X-ray	2.30	A	1-287	[»]
4F6X	X-ray	1.98	A	1-287	[»]

ProteinModelPortal

A9JQL9.

SMR

A9JQL9. Positions 1-284.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

UniPathway

UPA00029; UER00556.

Family and domain databases

Gene3D

1.10.600.10. 1 hit.

InterPro

IPR002060. Squ/phyt_synthse.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view]

Pfam

PF00494. SQS_PSY. 1 hit.
[Graphical view]

SUPFAM

SSF48576. Terpenoid_synth. 1 hit.

PROSITE

PS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

A9JQL9.

ChEMBL

CHEMBL5440.

EvolutionaryTrace

A9JQL9.

Entry information

Entry name

CRTM_STAAU

Accession

Primary (citable) accession number: A9JQL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	February 5, 2008
Last modified:	March 6, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program