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P37269 (CRTB_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
All-trans-phytoene synthase

Short name=PSase
EC=2.5.1.99
Gene names
Name:crtB
Synonyms:pys
Ordered Locus Names:Synpcc7942_1984
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of carotenoids. Catalyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to give prephytoene diphosphate (PPPP) and the subsequent rearrangement of the cyclopropylcarbinyl intermediate to yield all-trans phytoene. Ref.1

Catalytic activity

2 geranylgeranyl diphosphate = all-trans-phytoene + 2 diphosphate. Ref.1

Cofactor

ATP. ATP is required for the transferase activity but it does not seem to be hydrolyzed during the reaction By similarity.

Manganese or magnesium By similarity.

Pathway

Carotenoid biosynthesis; phytoene biosynthesis; all-trans-phytoene from geranylgeranyl diphosphate: step 1/1.

Sequence similarities

Belongs to the phytoene/squalene synthase family.

Ontologies

Keywords
   Biological processCarotenoid biosynthesis
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcarotenoid biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functiongeranylgeranyl-diphosphate geranylgeranyltransferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308All-trans-phytoene synthase
PRO_0000067437

Experimental info

Sequence conflict2491G → C Ref.1
Sequence conflict251 – 2522RQ → E Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37269 [UniParc].

Last modified April 18, 2006. Version 2.
Checksum: 9399E7308C4FFC18

FASTA30835,891
        10         20         30         40         50         60 
MLQMIPARPS RALASLSEAY EECRQITARY AKTFYLGTLL MPEAKRQAIW AIYVWCRRTD 

        70         80         90        100        110        120 
ELVDGPQAAQ TNFATLDAWE RRLERLFAGE PEDDCDVALV DTLARYPLDI QPFRDMIEGQ 

       130        140        150        160        170        180 
RMDLLQNRYS TFEDLYTYCY RVAGTVGLMS QPVMGIESTN SRAPWDPTTP PDPTQEALAL 

       190        200        210        220        230        240 
GIANQLTNIL RDVGEDARRG RIYLPQEELA QFNYSEQDLF NGVIDDRWRA FMQFQLDRAR 

       250        260        270        280        290        300 
DYFEQAERGI RQLSHDARWP VWASLMLYRE ILDVIEQNNY DVFRKRAYVP TWRKLCSLPV 


AMLRATVL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression in Escherichia coli of a cyanobacterial gene coding for phytoene synthase, a carotenoid biosynthesis enzyme."
Chamovitz D., Misawa D., Sandmann N., Hirshberg J.
FEBS Lett. 296:305-310(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63873 Genomic DNA. Translation: CAA45350.1.
CP000100 Genomic DNA. Translation: ABB58014.1.
PIRS20383.
RefSeqYP_401001.1. NC_007604.1.

3D structure databases

ProteinModelPortalP37269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_1984.

Protocols and materials databases

DNASU3774171.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB58014; ABB58014; Synpcc7942_1984.
GeneID3774171.
KEGGsyf:Synpcc7942_1984.
PATRIC23789427. VBISynElo51371_2236.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1562.
HOGENOMHOG000220848.
KOK02291.
OrthoDBEOG63FW00.
ProtClustDBCLSK893015.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_1984-MONOMER.
UniPathwayUPA00799; UER00773.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
InterProIPR002060. Squ/phyt_synthse.
IPR019845. Squalene/phytoene_synthase_CS.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMSSF48576. SSF48576. 1 hit.
PROSITEPS01044. SQUALEN_PHYTOEN_SYN_1. 1 hit.
PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCRTB_SYNE7
AccessionPrimary (citable) accession number: P37269
Secondary accession number(s): Q31LQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 18, 2006
Last modified: November 13, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways