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Protein

4,4'-diapophytoene synthase

Gene

crtM

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the yellow-orange carotenoid staphyloxanthin, which plays a role in the virulence via its protective function against oxidative stress. Catalyzes the head-to-head condensation of two molecules of farnesyl diphosphate (FPP) into the colorless C(30) carotenoid 4,4'-diapophytoene (dehydrosqualene).1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 2 Mg2+ ions per subunit. A third Mg2+ ion binds between the 2 farnesyl diphosphate (FPP).1 Publication

Pathwayi: staphyloxanthin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes staphyloxanthin from farnesyl diphosphate.Curated
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. 4,4'-diapophytoene 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 1Combined sources1 Publication1
Binding sitei45Farnesyl diphosphate 1Combined sources1 Publication1
Binding sitei45Farnesyl diphosphate 2Combined sources1 Publication1
Metal bindingi48Magnesium 1Combined sources1 Publication1
Metal bindingi52Magnesium 1Combined sources1 Publication1
Binding sitei165Farnesyl diphosphate 2Combined sources1 Publication1
Metal bindingi168Magnesium 2Combined sources1 Publication1
Binding sitei171Farnesyl diphosphate 1Combined sources1 Publication1
Metal bindingi172Magnesium 2Combined sources1 Publication1
Binding sitei248Farnesyl diphosphate 1Combined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processCarotenoid biosynthesis, Virulence
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDAi2.5.1.96 3352
UniPathwayiUPA00029; UER00556

Names & Taxonomyi

Protein namesi
Recommended name:
4,4'-diapophytoene synthaseBy similarity (EC:2.5.1.961 Publication)
Short name:
DAP synthaseBy similarity
Alternative name(s):
C30 carotenoid synthaseBy similarity
Dehydrosqualene synthase1 Publication
Gene namesi
Name:crtM1 Publication
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5440
DrugBankiDB07420 (1R)-4-(3-phenoxyphenyl)-1-phosphonobutane-1-sulfonic acid
DB04695 FARNESYL THIOPYROPHOSPHATE
DB07424 tripotassium (1R)-4-biphenyl-4-yl-1-phosphonatobutane-1-sulfonate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003473351 – 2874,4'-diapophytoene synthaseAdd BLAST287

Interactioni

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 – 21Farnesyl diphosphate 1 bindingCombined sources1 Publication4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105FE1 Bacteria
COG1562 LUCA

Family and domain databases

CDDicd00683 Trans_IPPS_HH, 1 hit
Gene3Di1.10.600.10, 1 hit
InterProiView protein in InterPro
IPR008949 Isoprenoid_synthase_dom_sf
IPR002060 Squ/phyt_synthse
IPR019845 Squalene/phytoene_synthase_CS
IPR033904 Trans_IPPS_HH
PfamiView protein in Pfam
PF00494 SQS_PSY, 1 hit
SUPFAMiSSF48576 SSF48576, 1 hit
PROSITEiView protein in PROSITE
PS01044 SQUALEN_PHYTOEN_SYN_1, 1 hit

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_NXFH01000003.1

Similar proteinsi

Entry informationi

Entry nameiCRTM_STAAU
AccessioniPrimary (citable) accession number: A9JQL9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 5, 2008
Last modified: April 25, 2018
This is version 53 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure
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Main funding by: National Institutes of Health