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Protein

All-trans-phytoene synthase/15-cis-phytoene synthase

Gene

crtB

Organism
Pantoea ananas (Erwinia uredovora)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 both 15-cis and all-trans phytoene isomers.1 Publication

Catalytic activityi

2 geranylgeranyl diphosphate = all-trans-phytoene + 2 diphosphate.1 Publication
2 geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by phosphate ions and squalestatin.1 Publication

Kineticsi

  1. KM=41 µM for GGPP (at pH 8 and 37 degrees Celsius)1 Publication

    Pathway: phytoene biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes all-trans-phytoene from geranylgeranyl diphosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. All-trans-phytoene synthase/15-cis-phytoene synthase (crtB)
    This subpathway is part of the pathway phytoene 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 all-trans-phytoene from geranylgeranyl diphosphate, the pathway phytoene biosynthesis and in Carotenoid biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    • carotenoid biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carotenoid biosynthesis

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00799; UER00773.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    All-trans-phytoene synthase/15-cis-phytoene synthase (EC:2.5.1.32, EC:2.5.1.99)
    Short name:
    PSase
    Gene namesi
    Name:crtB
    OrganismiPantoea ananas (Erwinia uredovora)
    Taxonomic identifieri553 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoea

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 309309All-trans-phytoene synthase/15-cis-phytoene synthasePRO_0000067429Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi706191.PANA_4162.

    Structurei

    3D structure databases

    ProteinModelPortaliP21683.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phytoene/squalene synthase family.Curated

    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.
    PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21683-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNNPSLLNHA VETMAVGSKS FATASKLFDA KTRRSVLMLY AWCRHCDDVI
    60 70 80 90 100
    DDQTLGFQAR QPALQTPEQR LMQLEMKTRQ AYAGSQMHEP AFAAFQEVAM
    110 120 130 140 150
    AHDIAPAYAF DHLEGFAMDV REAQYSQLDD TLRYCYHVAG VVGLMMAQIM
    160 170 180 190 200
    GVRDNATLDR ACDLGLAFQL TNIARDIVDD AHAGRCYLPA SWLEHEGLNK
    210 220 230 240 250
    ENYAAPENRQ ALSRIARRLV QEAEPYYLSA TAGLAGLPLR SAWAIATAKQ
    260 270 280 290 300
    VYRKIGVKVE QAGQQAWDQR QSTTTPEKLT LLLAASGQAL TSRMRAHPPR

    PAHLWQRPL
    Length:309
    Mass (Da):34,472
    Last modified:May 16, 2003 - v2
    Checksum:i9AA381A7376BBFC9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D90087 Genomic DNA. Translation: BAA14128.2.
    PIRiE37802.
    RefSeqiWP_013027995.1. NZ_JMJK01000017.1.

    Genome annotation databases

    GeneIDi11794608.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D90087 Genomic DNA. Translation: BAA14128.2.
    PIRiE37802.
    RefSeqiWP_013027995.1. NZ_JMJK01000017.1.

    3D structure databases

    ProteinModelPortaliP21683.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi706191.PANA_4162.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi11794608.

    Enzyme and pathway databases

    UniPathwayiUPA00799; UER00773.

    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.
    PS01045. SQUALEN_PHYTOEN_SYN_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli."
      Misawa N., Nakagawa M., Kobayashi K., Yamano S., Izawa Y., Nakamura K., Harashima K.
      J. Bacteriol. 172:6704-6712(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 20D3.
    2. Misawa N., Nakagawa M., Kobayashi K., Yamano S., Izawa Y., Nakamura K., Harashima K.
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO N-TERMINUS.
    3. "Expression of an active phytoene synthase from Erwinia uredovora and biochemical properties of the enzyme."
      Neudert U., Martinez-Ferez I.M., Fraser P.D., Sandmann G.
      Biochim. Biophys. Acta 1392:51-58(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.

    Entry informationi

    Entry nameiCRTB_PANAN
    AccessioniPrimary (citable) accession number: P21683
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 16, 2003
    Last modified: June 24, 2015
    This is version 71 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.