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Protein

Probable GDP-L-fucose synthase

Gene

Gmer

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.By similarity

Catalytic activityi

GDP-beta-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-alpha-D-mannose + NADPH.

Pathwayi: GDP-L-fucose biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. GDP-mannose 4,6 dehydratase (Gmd)
  2. Probable GDP-L-fucose synthase (Gmer)
This subpathway is part of the pathway GDP-L-fucose biosynthesis via de novo pathway, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose, the pathway GDP-L-fucose biosynthesis via de novo pathway and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei107 – 1071Important for catalytic activityBy similarity
Sitei109 – 1091Important for catalytic activityBy similarity
Active sitei136 – 1361Proton donor/acceptorBy similarity
Binding sitei140 – 1401NADPBy similarity
Sitei140 – 1401Lowers pKa of active site TyrBy similarity
Binding sitei179 – 1791NADPBy similarity
Binding sitei187 – 1871SubstrateBy similarity
Binding sitei215 – 2151SubstrateBy similarity
Binding sitei277 – 2771SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 147NADPBy similarity
Nucleotide bindingi163 – 1664NADPBy similarity

GO - Molecular functioni

  • coenzyme binding Source: InterPro
  • GDP-L-fucose synthase activity Source: FlyBase
  • isomerase activity Source: UniProtKB-KW

GO - Biological processi

  • 'de novo' GDP-L-fucose biosynthetic process Source: UniProtKB-UniPathway
  • dsRNA transport Source: FlyBase
  • GDP-L-fucose biosynthetic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.271. 1994.
ReactomeiR-DME-6787639. GDP-fucose biosynthesis.
UniPathwayiUPA00128; UER00191.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable GDP-L-fucose synthase (EC:1.1.1.271)
Alternative name(s):
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
Protein FX
Gene namesi
Name:Gmer
ORF Names:CG3495
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0267823. Gmer.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Probable GDP-L-fucose synthasePRO_0000174353Add
BLAST

Proteomic databases

PaxDbiQ9W1X8.
PRIDEiQ9W1X8.

Expressioni

Gene expression databases

BgeeiQ9W1X8.
ExpressionAtlasiQ9W1X8. differential.
GenevisibleiQ9W1X8. DM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi7227.FBpp0071816.

Structurei

3D structure databases

ProteinModelPortaliQ9W1X8.
SMRiQ9W1X8. Positions 3-321.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1431. Eukaryota.
COG0451. LUCA.
GeneTreeiENSGT00390000004681.
InParanoidiQ9W1X8.
KOiK02377.
OMAiIYRADFI.
OrthoDBiEOG7C5M8M.
PhylomeDBiQ9W1X8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00956. GDP_fucose_synth.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR028614. GDP_fucose/colitose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9W1X8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVLVTGGT GLVGKALEAV IKEQSPEDEQ WFFAGSKDAD LTNLAATQAL
60 70 80 90 100
FAREKPTHVI HLAAMVGGLF HNMNNNLDFL RNNLLINDNV LQTAHEQGCV
110 120 130 140 150
KVVSCLSTCI FPDKTSYPID ETMVHNGPPH PSNYGYSYAK RLIDVQNHAY
160 170 180 190 200
HDKYGRVYTS VIPCNIFGPH DNYNPEVSHV IPGMIYRMHQ LVTEKTDVPE
210 220 230 240 250
NDKVFTVFGS GMPLRQFVYS RDLAELMIWV LRNYESVEPI ILSADEVQEV
260 270 280 290 300
TIFEVAQAVA KAFNFNGRLV CDTSKSDGQY KKTASNAKLR SFLPDYAFTD
310 320
LETAINASVK WYIENYDQAR K
Length:321
Mass (Da):36,123
Last modified:May 1, 2000 - v1
Checksum:iE4167CE378D2D8E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121P → R in AAM51008 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM231688 mRNA. Translation: CAJ77751.1.
AE013599 Genomic DNA. Translation: AAF46924.1.
AY060873 mRNA. Translation: AAL28421.1.
AY119148 mRNA. Translation: AAM51008.1.
RefSeqiNP_611734.1. NM_137890.3.
UniGeneiDm.739.

Genome annotation databases

EnsemblMetazoaiFBtr0071905; FBpp0071816; FBgn0034794.
GeneIDi37638.
KEGGidme:Dmel_CG3495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM231688 mRNA. Translation: CAJ77751.1.
AE013599 Genomic DNA. Translation: AAF46924.1.
AY060873 mRNA. Translation: AAL28421.1.
AY119148 mRNA. Translation: AAM51008.1.
RefSeqiNP_611734.1. NM_137890.3.
UniGeneiDm.739.

3D structure databases

ProteinModelPortaliQ9W1X8.
SMRiQ9W1X8. Positions 3-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0071816.

Proteomic databases

PaxDbiQ9W1X8.
PRIDEiQ9W1X8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071905; FBpp0071816; FBgn0034794.
GeneIDi37638.
KEGGidme:Dmel_CG3495.

Organism-specific databases

CTDi37638.
FlyBaseiFBgn0267823. Gmer.

Phylogenomic databases

eggNOGiKOG1431. Eukaryota.
COG0451. LUCA.
GeneTreeiENSGT00390000004681.
InParanoidiQ9W1X8.
KOiK02377.
OMAiIYRADFI.
OrthoDBiEOG7C5M8M.
PhylomeDBiQ9W1X8.

Enzyme and pathway databases

UniPathwayiUPA00128; UER00191.
BRENDAi1.1.1.271. 1994.
ReactomeiR-DME-6787639. GDP-fucose biosynthesis.

Miscellaneous databases

GenomeRNAii37638.
NextBioi804682.
PROiQ9W1X8.

Gene expression databases

BgeeiQ9W1X8.
ExpressionAtlasiQ9W1X8. differential.
GenevisibleiQ9W1X8. DM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00956. GDP_fucose_synth.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR028614. GDP_fucose/colitose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Reconstitution in vitro of the GDP-fucose biosynthetic pathways of Caenorhabditis elegans and Drosophila melanogaster."
    Rhomberg S., Fuchsluger C., Rendic D., Paschinger K., Jantsch V., Kosma P., Wilson I.B.H.
    FEBS J. 273:2244-2256(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication and Ovary1 Publication.
  5. "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism."
    Roos C., Kolmer M., Mattila P., Renkonen R.
    J. Biol. Chem. 277:3168-3175(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMOLOGY.

Entry informationi

Entry nameiFCL_DROME
AccessioniPrimary (citable) accession number: Q9W1X8
Secondary accession number(s): Q1H8X1, Q8MS16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.