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Protein

Bifunctional lycopene cyclase/phytoene synthase

Gene

An07g00800

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase).By similarity

Catalytic activityi

Carotenoid psi-end group = carotenoid beta-end group.
2 geranylgeranyl diphosphate = 15-cis-phytoene + 2 diphosphate.

Pathway:ibeta-carotene biosynthesis

This protein is involved in the pathway beta-carotene biosynthesis, which is part of Carotenoid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway beta-carotene biosynthesis and in Carotenoid biosynthesis.

Pathway:iphytoene 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. Bifunctional lycopene cyclase/phytoene synthase (An07g00800)
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

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Transferase

Keywords - Biological processi

Carotenoid biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00799; UER00773.
UPA00802.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional lycopene cyclase/phytoene synthase
Including the following 2 domains:
Lycopene beta-cyclase (EC:5.5.1.19)
Alternative name(s):
Lycopene cyclase
Phytoene synthase (EC:2.5.1.32)
Gene namesi
ORF Names:An07g00800
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706 Componenti: Chromosome 4L

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei34 – 5421HelicalSequence AnalysisAdd
BLAST
Transmembranei59 – 7921HelicalSequence AnalysisAdd
BLAST
Transmembranei99 – 12123HelicalSequence AnalysisAdd
BLAST
Transmembranei142 – 16221HelicalSequence AnalysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence AnalysisAdd
BLAST
Transmembranei242 – 26221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582Bifunctional lycopene cyclase/phytoene synthasePRO_0000409232Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA2QM49.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 261261Lycopene beta-cyclaseAdd
BLAST
Regioni268 – 582315Phytoene synthaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the lycopene beta-cyclase family.Curated
In the C-terminal section; belongs to the phytoene/squalene synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47964.
OrthoDBiEOG7RBZJ2.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR017825. Lycopene_cyclase_dom.
IPR002060. Squ/phyt_synthse.
[Graphical view]
PfamiPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
TIGRFAMsiTIGR03462. CarR_dom_SF. 2 hits.

Sequencei

Sequence statusi: Complete.

A2QM49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQNGTRLCY SVREVPPTSF VSAPANYKRA SSHCTYTIPA ASALTVLYYP
60 70 80 90 100
FFTAQDRCKI CILITIAILA TLPWDSYLIR SAIWTYPPDA VVGLKILDIP
110 120 130 140 150
IEEVFFFAIQ TYITSLTYCI FTKPLVRPMY LRSHLERRGT RYVVATVILA
160 170 180 190 200
LMGGGTACLL LGRRMTYLGL ILVWACPILL FQWMMSYPFL SELPWKPTIT
210 220 230 240 250
SICLPTLHLW FADSRAMGTG TWRIEEGTKL NFRIGGLELE EALFFLVSNM
260 270 280 290 300
MVVLGLVGCD YAYALQEYES LSQPASDVYI TLRKALSLLA RPLPIDASLI
310 320 330 340 350
SALSQAVYRL QEKSQSMFLG SALFQGQLRI DLIFLYSFCR VMDDLIDEAE
360 370 380 390 400
DEQEARFWVT ECRHLLDSTH RSEPHSDHFY TGKKGEEHER LRQSISYLPP
410 420 430 440 450
SHLSNDSFDD LLKGFEIDLK FNPQREAFPI QSEYCLDQYA GFVAGTVGVL
460 470 480 490 500
VFDLTLFHCG HYFIQDVPRL RRAAKDMGKA MQCQPRGDGG ATSGRKRAIA
510 520 530 540 550
GNRGELYGYW TTAEGAERHK PGASVEDEGA FGATAKSWLA GDVITELCHC
560 570 580
FIQAEYVIYL VRHQNASADT LVLLSALVYR LE
Length:582
Mass (Da):65,647
Last modified:March 6, 2007 - v1
Checksum:i88E8322BC29400BA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270119 Genomic DNA. Translation: CAK39303.1.

Genome annotation databases

EnsemblFungiiCADANGAT00005357; CADANGAP00005250; CADANGAG00005357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270119 Genomic DNA. Translation: CAK39303.1.

3D structure databases

ProteinModelPortaliA2QM49.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00005357; CADANGAP00005250; CADANGAG00005357.

Phylogenomic databases

eggNOGiNOG47964.
OrthoDBiEOG7RBZJ2.

Enzyme and pathway databases

UniPathwayiUPA00799; UER00773.
UPA00802.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR017825. Lycopene_cyclase_dom.
IPR002060. Squ/phyt_synthse.
[Graphical view]
PfamiPF00494. SQS_PSY. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
TIGRFAMsiTIGR03462. CarR_dom_SF. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiLCPS_ASPNC
AccessioniPrimary (citable) accession number: A2QM49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: March 6, 2007
Last modified: June 24, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

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.