Reviewed, UniProtKB/Swiss-Prot Q1ZXF7 (GMDS_DICDI)

Names and origin

Protein names

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

Gene names

Name:	gmd
ORF Names:	DDB_G0284553

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	NADP
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	GDP-mannose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	GDP-mannose 4,6-dehydratase activity Inferred from electronic annotation. Source: EC 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 – 356	356	GDP-mannose 4,6 dehydratase		PRO_0000327628
Sites
	Active site	138	1	By similarity
	Active site	140	1	Nucleophile By similarity
	Active site	162	1	Nucleophile By similarity
	Binding site	166	1	NADP By similarity
Natural variations
	Natural variant	108	1	G → D in strain: HL250; loss of activity.

Sequences

	Sequence		Length	Mass (Da)
	Q1ZXF7-1 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: 9DB1B513B28E16CA	FASTA	356	41,061
	10 20 30 40 50 60 MSEERKVALI TGITGQDGSY LTEFLISKGY YVHGIIQKIF HHFNTIVKNI YIKIDMLKEK 70 80 90 100 110 120 ESLTLHYGDL TDASNLHSIV SKVNPTEIYN LGAQSHVKVS FDMSEYTGDV DGLGCLRLLD 130 140 150 160 170 180 AIRSCGMEKK VKYYQASTSE LYGKVQEIPQ SETTPFYPRS PYAVAKQYAY WIVVNYREAY 190 200 210 220 230 240 DMYACNGILF NHESPRRGPT FVTRKITRFV AGIACGRDEI LYLGNINAKR DWGHARDYVE 250 260 270 280 290 300 AMWLMLQQEK PEDFVIATGE THSVREFVEK SFKEIDIIIK WRGEAEKEEG YCEKTGKVYV 310 320 330 340 350 KIDEKYYRPT EVDLLLGNPN KAKKLLQWQI KTSFGELVKE MVAKDIEYIK NGDKYN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Development of Dictyostelium discoideum is associated with alteration of fucosylated N-glycan structures." Schiller B., Hykollari A., Voglmeir J., Poltl G., Hummel K., Razzazi-Fazeli E., Geyer R., Wilson I.B.H. Biochem. J. 423:41-52(2009) [PubMed: 19614564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION. Strain: HL250.
[2]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000066 Genomic DNA. Translation: EAS66860.1.
RefSeq	XP_001134543.1.
3D structure databases
SMR	Q1ZXF7. Positions 5-350.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1ZXF7.
Genome annotation databases
GeneID	8624624.
KEGG	ddi:DDB_0231676.
Organism-specific databases
dictyBase	DDB_G0284553. gmd.
Phylogenomic databases
eggNOG	KOG1372.
HOGENOM	HBG755066.
OMA	TQRVDHI.
PhylomeDB	Q1ZXF7.
Enzyme and pathway databases
BRENDA	4.2.1.47. 424.
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...

Entry information

Entry name

GMDS_DICDI

Accession

Primary (citable) accession number: Q1ZXF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 2, 2006
Last modified:	February 9, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)