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Protein

GDP-mannose 4,6 dehydratase 2

Gene

MUR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

GTP-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

TAIRiAT3G51160.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

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

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.
OMAiCEAAFGH.
OrthoDBiEOG09360CC2.
PhylomeDBiP93031.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00955. GDP_Man_dehydratase. 1 hit.
InterProiIPR006368. GDP_Man_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi9598. 3 interactors.
STRINGi3702.AT3G51160.1.

PTM databases

iPTMnetiP93031.

Proteomic databases

PaxDbiP93031.
PRIDEiP93031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G51160.

Phylogenomic databases

eggNOGiKOG1372. Eukaryota.
COG1089. LUCA.
HOGENOMiHOG000168003.
InParanoidiP93031.
KOiK01711.
OMAiCEAAFGH.
OrthoDBiEOG09360CC2.
PhylomeDBiP93031.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP93031.
PROiP93031.

Gene expression databases

GenevisibleiP93031. AT.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00955. GDP_Man_dehydratase. 1 hit.
InterProiIPR006368. GDP_Man_deHydtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF16363. GDP_Man_Dehyd. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01472. gmd. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGMD2_ARATH
AccessioniPrimary (citable) accession number: P93031
Secondary accession number(s): Q1ECM4, Q8LFY4, Q9SD30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 22, 2005
Last modified: November 30, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.