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Q8K3X3 (GMDS_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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=GMD
Gene names
Name:GMDS
Synonyms:GMD
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

NADP By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 372371GDP-mannose 4,6 dehydratase
PRO_0000201704

Sites

Active site1551 By similarity
Active site1571Nucleophile By similarity
Active site1791Nucleophile By similarity
Binding site1831NADP By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K3X3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: D4E256DF97230D2E

FASTA37241,974
        10         20         30         40         50         60 
MAHAPASCPS SRNSGDGDKG KPRKVALITG ITGQDGSYLA EFLLEKGYEV HGIVRRSSSF 

        70         80         90        100        110        120 
NTGRIEHLYK NPQAHIEGNM KLHYGDLTDS TCLVKIINEV KPTEIYNLGA QSHVKISFDL 

       130        140        150        160        170        180 
AEYTADVDGV GTLRLLDAIK TCGLINSVKF YQASTSELYG KVQEIPQKET TPFYPRSPYG 

       190        200        210        220        230        240 
AAKLYAYWIV VNFREAYNLF AVNGILFNHE SPRRGANFVT RKISRSVAKI YLGQLECFSL 

       250        260        270        280        290        300 
GNLDAKRDWG HAKDYVEAMW LMLQNDEPED FVIATGEVHS VREFVEKSFM HIGKTIVWEG 

       310        320        330        340        350        360 
KNENEVGRCK ETGKIHVTVD LKYYRPTEVD FLQGDCSKAQ QKLNWKPRVA FDELVREMVQ 

       370 
ADVELMRTNP NA 

« Hide

References

[1]"Glycan-dependent regulation of GDP-mannose 4,6-dehydratase activity."
Becker D.J., Smith P.L., Petryniak B., Kelly R.J., Myers J.T., Wu B., Wang P.G., Lowe J.B.
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF525364 mRNA. Translation: AAM91925.1.
RefSeqNP_001233625.1. NM_001246696.1.

3D structure databases

ProteinModelPortalQ8K3X3.
SMRQ8K3X3. Positions 23-369.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689436.

Phylogenomic databases

HOVERGENHBG000727.

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.
PANTHERPTHR10366:SF32. GDP_mann_dehyd. 1 hit.
PfamPF01370. Epimerase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01472. Gmd. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGMDS_CRIGR
AccessionPrimary (citable) accession number: Q8K3X3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families