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Q9VMW9 (GMDS_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GDP-mannose 4,6 dehydratase
EC=4.2.1.47
Alternative name(s):
GDP-D-mannose dehydratase
Short name=Dm-gmd
Gene names
Name:Gmd
ORF Names:CG8890
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conversion of GDP-D-mannose to GDP-4-keto-6-D-deoxymannose. Ref.1

Catalytic activity

GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H2O.

Cofactor

NADP. Ref.1

Pathway

Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.

Sequence similarities

Belongs to the GDP-mannose 4,6-dehydratase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5-8. Ref.1

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395GDP-mannose 4,6 dehydratase
PRO_0000201707

Sites

Active site1781 By similarity
Active site1801Nucleophile By similarity
Active site2021Nucleophile By similarity
Binding site2061NADP By similarity

Experimental info

Sequence conflict3331N → S in CAJ77750. Ref.1
Sequence conflict3331N → S in AAL90257. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9VMW9 [UniParc].

Last modified July 25, 2003. Version 2.
Checksum: 533E1B41E69ED36D

FASTA39544,784
        10         20         30         40         50         60 
MLNTRLIAMS TSDGAPETKK QRPESSSNGS KDQNGTEAGA EGDSRDKVAL ITGITGQDGS 

        70         80         90        100        110        120 
YLAEFLLKKD YEVHGIIRRA STFNTTRIEH LYADPKAHKG GRMKLHYGDM TDSSSLVKII 

       130        140        150        160        170        180 
NMVKPTEIYN LAAQSHVKVS FDLSEYTAEV DAVGTLRILD AIRTCGMEKN VRFYQASTSE 

       190        200        210        220        230        240 
LYGKVVETPQ NEQTPFYPRS PYACAKMYGF WIVINYREAY NMYACNGILF NHESPRRGEN 

       250        260        270        280        290        300 
FVTRKITRSV AKIYHKQMEY FELGNLDSKR DWGHASDYVE AMWMMLQRES PSDYVIATGE 

       310        320        330        340        350        360 
THSVREFVEA AFKHIDREIT WKGKGVDEVG VENGTGIVRV RINPKYFRPT EVDLLQGDAS 

       370        380        390 
KANRELNWTP KVTFVELVSD MMKADIELMR KNPIA

« Hide

References

« Hide 'large scale' references
[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: 16650000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Ovary.
[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: 11698403] [Abstract]
Cited for: HOMOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM231687 mRNA. Translation: CAJ77750.1.
AE014134 Genomic DNA. Translation: AAF52189.2.
AY089519 mRNA. Translation: AAL90257.1.
RefSeqNP_608888.2. NM_135044.3.
UniGeneDm.4967.

3D structure databases

ProteinModelPortalQ9VMW9.
SMRQ9VMW9. Positions 48-392.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9VMW9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079049; FBpp0078685; FBgn0031661.
GeneID33716.
KEGGdme:Dmel_CG8890.
NMPDRfig|7227.3.peg.800.

Organism-specific databases

CTD33716.
FlyBaseFBgn0031661. Gmd.

Phylogenomic databases

eggNOGinNOG06546.
GeneTreeEMGT00050000011127.
InParanoidQ9VMW9.
OMAEWAFADV.
OrthoDBEOG40K6FB.
PhylomeDBQ9VMW9.

Gene expression databases

BgeeQ9VMW9.
GermOnlineCG8890. Drosophila melanogaster.

Family and domain databases

InterProIPR001509. Epimerase_deHydtase.
IPR006368. GDP_Man_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK01711.
PANTHERPTHR10366:SF32. GDP_mann_dehyd. 1 hit.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01472. Gmd. 1 hit.
ProtoNetSearch...

Other

NextBio784930.

Entry information

Entry nameGMDS_DROME
AccessionPrimary (citable) accession number: Q9VMW9
Secondary accession number(s): Q1H8X2, Q8T3U5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 25, 2003
Last modified: January 25, 2012
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents