Reviewed, UniProtKB/Swiss-Prot O45583 (GMD2_CAEEL)

Names and origin

Protein names

Recommended name:
    GDP-mannose 4,6 dehydratase 2
    EC=4.2.1.47
Alternative name(s):
    GDP-D-mannose dehydratase
      Short name=GMD

Gene names

Name:	gmd-2
ORF Names:	F56H6.5

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conversion of GDP-D-mannose to GDP-4-keto-6-D-deoxymannose. Ref.2
Catalytic activity	GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H2O. Ref.2
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.
Developmental stage	Expressed throughout development. Ref.2
Sequence similarities	Belongs to the GDP-mannose 4,6-dehydratase family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 16-23 degrees Celsius.

Ontologies

Keywords
Ligand	NADP
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	GDP-mannose metabolic process Ref.2 Inferred from direct assay. Source: UniProtKB body morphogenesis Inferred from mutant phenotype. Source: WormBase growth Inferred from mutant phenotype. Source: WormBase locomotion Inferred from mutant phenotype. Source: WormBase nematode larval development Inferred from mutant phenotype. Source: WormBase oviposition Inferred from mutant phenotype. Source: WormBase
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	GDP-mannose 4,6-dehydratase activity Ref.2 Inferred from direct assay. Source: UniProtKB coenzyme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	GDP-mannose 4,6 dehydratase 2		PRO_0000201709
Sites
	Active site	166	1	By similarity
	Active site	168	1	Nucleophile By similarity
	Active site	190	1	Nucleophile By similarity
	Binding site	194	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O45583-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 1A3437F87872B457	FASTA	382	43,071
	10 20 30 40 50 60 MEARNAEGLE SCIEKIQEVK LSSFAELKAF RERKVALITG ITGQDGSYLA ELLLSKGYKV 70 80 90 100 110 120 HGIIRRSSSF NTARIEHLYG NPVTHNGSAS FSLHYGDMTD SSCLIKLIST IEPTEIYHLA 130 140 150 160 170 180 AQSHVKVSFD LPEYTAEVDA VGTLRLLDAI HACRLTEKVR FYQASTSELY GKVQEIPQSE 190 200 210 220 230 240 LTPFYPRSPY AVAKMYGYWI VVNYREAYKM FACNGILFNH ESPRRGETFV TRKITRSVAK 250 260 270 280 290 300 ISLRQQEHIE LGNLSALRDW GHAKEYVEAM WRILQQDTPD DFVIATGKQF SVREFCNLAF 310 320 330 340 350 360 AEIGEQLVWE GEGVDEVGKN QDGVVRVKVS PKYYRPTEVE TLLGNPAKAR KTLGWEPKIT 370 380 VPELVKEMVA SDIALMEADP MA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"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] OF 8-382, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z81553 Genomic DNA. Translation: CAB04494.1. AM231685 mRNA. Translation: CAJ77754.1.
PIR	T22798.
RefSeq	NP_493106.1.
UniGene	Cel.18597
3D structure databases
HSSP	HSSP built from PDB template 1DB3 based on UniProtKB P32054.
ModBase	Search...
Protein-protein interaction databases
IntAct	O45583. 1 interaction.
STRING	O45583.
Genome annotation databases
Ensembl	F56H6.5; F56H6.5; F56H6.5; Caenorhabditis elegans. [Genome view]
GeneID	186416.
KEGG	cel:F56H6.5.
UCSC	F56H6.5. c. elegans.
Organism-specific databases
CTD	186416.
WormBase	WBGene00010166. gmd-2.
WormPep	F56H6.5. CE16133. [WorfDB]
Phylogenomic databases
OMA	LANISQG.
Enzyme and pathway databases
BRENDA	4.2.1.47. 672.
Gene expression databases
ArrayExpress	O45583.
Family and domain databases
InterPro	IPR001509. Epimerase_deHydtase. IPR006368. GDP_Man_deHydtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR10366:SF32. GDP_mann_dehyd. 1 hit.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01472. gmd. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	931756.

Entry information

Entry name

GMD2_CAEEL

Accession

Primary (citable) accession number: O45583
Secondary accession number(s): Q1H8X4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project