Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GDP-mannose 4,6 dehydratase 2

Gene

MUR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose.2 Publications

Catalytic activityi

GDP-alpha-D-mannose = GDP-4-dehydro-alpha-D-rhamnose + H2O.1 Publication

Cofactori

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

This protein is involved in step 1 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 2 (MUR1), GDP-mannose 4,6 dehydratase 1 (GMD1)
  2. GDP-L-fucose synthase 1 (GER1), Putative GDP-L-fucose synthase 2 (GER2)
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)DescriptionActionsGraphical viewLength
Binding sitei60NADP1 Publication1
Binding sitei117Substrate; via carbonyl oxygen1 Publication1
Binding sitei128NADP1 Publication1
Active sitei1621 Publication1
Binding sitei162Substrate1 Publication1
Active sitei164Nucleophile1 Publication1
Active sitei185Nucleophile1 Publication1
Binding sitei185Substrate1 Publication1
Binding sitei189NADP1 Publication1
Binding sitei214Substrate1 Publication1
Binding sitei215NADP1 Publication1
Binding sitei220NADP1 Publication1
Binding sitei247Substrate; via amide nitrogen1 Publication1
Binding sitei253Substrate1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi35 – 40NADP1 Publication6
Nucleotide bindingi91 – 92NADP1 Publication2
Nucleotide bindingi113 – 117NADP1 Publication5

GO - Molecular functioni

  • GDP-mannose 4,6-dehydratase activity Source: TAIR
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • 'de novo' GDP-L-fucose biosynthetic process Source: TAIR
  • GDP-mannose metabolic process Source: InterPro
  • unidimensional cell growth Source: TAIR

Keywordsi

Molecular functionLyase
LigandGTP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G51160-MONOMER
MetaCyc:AT3G51160-MONOMER
BRENDAi4.2.1.47 399
ReactomeiR-ATH-6787639 GDP-fucose biosynthesis
UniPathwayiUPA00128; UER00190

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-mannose 4,6 dehydratase 2 (EC:4.2.1.47)
Alternative name(s):
GDP-D-mannose dehydratase 2
Short name:
GMD 2
Gene namesi
Name:MUR1
Synonyms:GMD2
Ordered Locus Names:At3g51160
ORF Names:F24M12.200
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

AraportiAT3G51160
TAIRilocus:2080933 AT3G51160

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107P → L in mur1-2; strong reduction in L-fucose in the cell walls. 1 Publication1
Mutagenesisi139R → C in mur1-7; strong reduction in L-fucose in the cell walls. 1 Publication1
Mutagenesisi153R → C in mur1-5; strong reduction in L-fucose in the cell walls. 1 Publication1
Mutagenesisi162S → F in mur1-1; strong reduction in L-fucose in the cell walls. 1 Publication1
Mutagenesisi191A → V in mur1-3; strong reduction in L-fucose in the cell walls. 1 Publication1
Mutagenesisi202A → V in mur1-6; strong reduction in L-fucose in the cell walls. 1 Publication1
Mutagenesisi210G → Q in mur1-4; strong reduction in L-fucose in the cell walls. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002017111 – 373GDP-mannose 4,6 dehydratase 2Add BLAST373

Proteomic databases

PaxDbiP93031
PRIDEiP93031

PTM databases

iPTMnetiP93031

Expressioni

Tissue specificityi

Expressed in roots, flowers, siliques, leaves and stems. Not expressed in the root meristem and the proximal part of the elongation zone, or in emerging lateral roots. Expressed in trichomes and guard cells, and in pollen just before anthesis.1 Publication

Gene expression databases

ExpressionAtlasiP93031 baseline and differential
GenevisibleiP93031 AT

Interactioni

Subunit structurei

Homotetramer. Binds to GER1.1 Publication

Protein-protein interaction databases

BioGridi9598, 3 interactors
STRINGi3702.AT3G51160.1

Structurei

Secondary structure

1373
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 34Combined sources5
Turni35 – 37Combined sources3
Helixi39 – 50Combined sources12
Beta strandi54 – 59Combined sources6
Turni68 – 73Combined sources6
Beta strandi85 – 89Combined sources5
Helixi95 – 105Combined sources11
Beta strandi108 – 112Combined sources5
Helixi119 – 124Combined sources6
Helixi126 – 133Combined sources8
Helixi135 – 151Combined sources17
Beta strandi156 – 162Combined sources7
Helixi163 – 166Combined sources4
Beta strandi171 – 173Combined sources3
Helixi184 – 203Combined sources20
Beta strandi206 – 212Combined sources7
Helixi225 – 237Combined sources13
Beta strandi244 – 247Combined sources4
Beta strandi252 – 254Combined sources3
Helixi258 – 269Combined sources12
Beta strandi271 – 273Combined sources3
Beta strandi276 – 279Combined sources4
Beta strandi284 – 286Combined sources3
Helixi287 – 297Combined sources11
Helixi302 – 304Combined sources3
Beta strandi306 – 308Combined sources3
Helixi310 – 312Combined sources3
Helixi326 – 332Combined sources7
Helixi340 – 363Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N7GX-ray2.20A/B/C/D1-373[»]
1N7HX-ray1.80A/B1-373[»]
ProteinModelPortaliP93031
SMRiP93031
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP93031

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni220 – 228Substrate binding1 Publication9
Regioni314 – 317Substrate binding1 Publication4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1372 Eukaryota
COG1089 LUCA
HOGENOMiHOG000168003
InParanoidiP93031
KOiK01711
OMAiTDCLYLG
OrthoDBiEOG09360CC2
PhylomeDBiP93031

Family and domain databases

HAMAPiMF_00955 GDP_Man_dehydratase, 1 hit
InterProiView protein in InterPro
IPR006368 GDP_Man_deHydtase
IPR016040 NAD(P)-bd_dom
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR43715 PTHR43715, 1 hit
PfamiView protein in Pfam
PF16363 GDP_Man_Dehyd, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01472 gmd, 1 hit

Sequencei

Sequence statusi: Complete.

P93031-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASENNGSRS DSESITAPKA DSTVVEPRKI ALITGITGQD GSYLTEFLLG
60 70 80 90 100
KGYEVHGLIR RSSNFNTQRI NHIYIDPHNV NKALMKLHYA DLTDASSLRR
110 120 130 140 150
WIDVIKPDEV YNLAAQSHVA VSFEIPDYTA DVVATGALRL LEAVRSHTID
160 170 180 190 200
SGRTVKYYQA GSSEMFGSTP PPQSETTPFH PRSPYAASKC AAHWYTVNYR
210 220 230 240 250
EAYGLFACNG ILFNHESPRR GENFVTRKIT RALGRIKVGL QTKLFLGNLQ
260 270 280 290 300
ASRDWGFAGD YVEAMWLMLQ QEKPDDYVVA TEEGHTVEEF LDVSFGYLGL
310 320 330 340 350
NWKDYVEIDQ RYFRPAEVDN LQGDASKAKE VLGWKPQVGF EKLVKMMVDE
360 370
DLELAKREKV LVDAGYMDAK QQP
Length:373
Mass (Da):41,961
Last modified:November 22, 2005 - v3
Checksum:i3AE1875B38BC1C82
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55V → F in AAM61140 (Ref. 5) Curated1
Sequence conflicti179 – 181FHP → IHL in CAB62638 (PubMed:11130713).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81805 mRNA Translation: AAB51505.1
AL132980 Genomic DNA Translation: CAB62638.1
CP002686 Genomic DNA Translation: AEE78758.1
BT025710 mRNA Translation: ABF82613.1
AY084574 mRNA Translation: AAM61140.1
PIRiT45747
RefSeqiNP_190685.2, NM_114976.4
UniGeneiAt.23910

Genome annotation databases

EnsemblPlantsiAT3G51160.1; AT3G51160.1; AT3G51160
GeneIDi824280
GrameneiAT3G51160.1; AT3G51160.1; AT3G51160
KEGGiath:AT3G51160

Similar proteinsi

Entry informationi

Entry nameiGMD2_ARATH
AccessioniPrimary (citable) accession number: P93031
Secondary accession number(s): Q1ECM4, Q8LFY4, Q9SD30
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 22, 2005
Last modified: April 25, 2018
This is version 132 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health