Q2FV59 · CRTM_STAA8

Function

function

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 C30 carotenoid 4,4'-diapophytoene (dehydrosqualene).

Miscellaneous

CrtM is not functional in a C40 pathway, however independent mutations on Phe-26, Trp-38 or Glu-180 are sufficient to permit the synthesis of C40 carotenoids, such as lycopene and 3,4,3',4'-tetrahydrolycopene, although there is a decrease in the synthesis of C30 compounds. The combination of mutations at Phe-26 and Trp-38 appears to be harmful for the general performance of the enzyme.
Upon coexpression with Erwinia geranylgeranyldiphosphate (GGDP) synthase, CrtM produces novel carotenoids with the asymmetrical C35 backbone, such as 4-apophytoene, and the production of the natural product 4,4'-diapophytoene drops dramatically.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 Mg2+ ions per subunit.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1.2 μMfarnesyl diphosphate
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
176 μM/h/mg

Pathway

Carotenoid biosynthesis; staphyloxanthin biosynthesis; staphyloxanthin from farnesyl diphosphate: step 1/5.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site18-21(2E,6E)-farnesyl diphosphate 1 (UniProtKB | ChEBI)
Binding site41(2E,6E)-farnesyl diphosphate 1 (UniProtKB | ChEBI)
Binding site45(2E,6E)-farnesyl diphosphate 1 (UniProtKB | ChEBI)
Binding site45(2E,6E)-farnesyl diphosphate 2 (UniProtKB | ChEBI)
Binding site48Mg2+ 1 (UniProtKB | ChEBI)
Binding site52Mg2+ 1 (UniProtKB | ChEBI)
Binding site165(2E,6E)-farnesyl diphosphate 2 (UniProtKB | ChEBI)
Binding site168Mg2+ 2 (UniProtKB | ChEBI)
Binding site171(2E,6E)-farnesyl diphosphate 1 (UniProtKB | ChEBI)
Binding site172Mg2+ 2 (UniProtKB | ChEBI)
Binding site248(2E,6E)-farnesyl diphosphate 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionfarnesyl-diphosphate farnesyltransferase activity
Molecular Functionfarnesyltranstransferase activity
Molecular Functiongeranylgeranyl-diphosphate geranylgeranyltransferase activity
Molecular Functionmetal ion binding
Biological Processcarotenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    4,4'-diapophytoene synthase
  • EC number
  • Short names
    DAP synthase
  • Alternative names
    • C30 carotenoid synthase
    • Dehydrosqualene synthase

Gene names

    • Name
      crtM
    • Ordered locus names
      SAOUHSC_02879

Organism names

Accessions

  • Primary accession
    Q2FV59

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis26Decrease in C30 carotene synthase activity. C40 carotene synthase activity acquired.
Mutagenesis26Decrease in C30 and C40 carotene synthase activities; when associated with A-38 or G-38.
Mutagenesis26Decrease in C30 and C40 carotene synthase activities; when associated with A-38 or G-38.
Mutagenesis38Decrease in C30 and C40 carotene synthase activities; when associated with A-26 or G-26.
Mutagenesis38Decrease in C30 carotene synthase activity. C40 carotene synthase activity acquired.
Mutagenesis38Decrease in C30 and C40 carotene synthase activities; when associated with A-26 or G-26.
Mutagenesis180Slight increase in C30 carotene synthase activity. C40 carotene synthase activity acquired.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002826161-2874,4'-diapophytoene synthase

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    287
  • Mass (Da)
    34,231
  • Last updated
    2006-03-21 v1
  • Checksum
    2407009413D42E63
MTMMDMNFKYCHKIMKKHSKSFSYAFDLLPEDQRKAVWAIYAVCRKIDDSIDVYGDIQFLNQIKEDIQSIEKYPYEHHHFQSDRRIMMALQHVAQHKNIAFQSFYNLIDTVYKDQHFTMFETDAELFGYCYGVAGTVGEVLTPILSDHETHQTYDVARRLGESLQLINILRDVGEDFDNERIYFSKQRLKQYEVDIAEVYQNGVNNHYIDLWEYYAAIAEKDFQDVMDQIKVFSIEAQPIIELAARIYIEILDEVRQANYTLHERVFVDKRKKAKLFHEINSKYHRI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000253
EMBL· GenBank· DDBJ
ABD31876.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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