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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601NADP1 Publication
Binding sitei117 – 1171Substrate; via carbonyl oxygen1 Publication
Binding sitei128 – 1281NADP1 Publication
Active sitei162 – 16211 Publication
Binding sitei162 – 1621Substrate1 Publication
Active sitei164 – 1641Nucleophile1 Publication
Active sitei185 – 1851Nucleophile1 Publication
Binding sitei185 – 1851Substrate1 Publication
Binding sitei189 – 1891NADP1 Publication
Binding sitei214 – 2141Substrate1 Publication
Binding sitei215 – 2151NADP1 Publication
Binding sitei220 – 2201NADP1 Publication
Binding sitei247 – 2471Substrate; via amide nitrogen1 Publication
Binding sitei253 – 2531Substrate1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 406NADP1 Publication
Nucleotide bindingi91 – 922NADP1 Publication
Nucleotide bindingi113 – 1175NADP1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071P → L in mur1-2; strong reduction in L-fucose in the cell walls. 1 Publication
Mutagenesisi139 – 1391R → C in mur1-7; strong reduction in L-fucose in the cell walls. 1 Publication
Mutagenesisi153 – 1531R → C in mur1-5; strong reduction in L-fucose in the cell walls. 1 Publication
Mutagenesisi162 – 1621S → F in mur1-1; strong reduction in L-fucose in the cell walls. 1 Publication
Mutagenesisi191 – 1911A → V in mur1-3; strong reduction in L-fucose in the cell walls. 1 Publication
Mutagenesisi202 – 2021A → V in mur1-6; strong reduction in L-fucose in the cell walls. 1 Publication
Mutagenesisi210 – 2101G → Q in mur1-4; strong reduction in L-fucose in the cell walls. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373GDP-mannose 4,6 dehydratase 2PRO_0000201711Add
BLAST

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 interactions.
STRINGi3702.AT3G51160.1.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 345Combined sources
Turni35 – 373Combined sources
Helixi39 – 5012Combined sources
Beta strandi54 – 596Combined sources
Turni68 – 736Combined sources
Beta strandi85 – 895Combined sources
Helixi95 – 10511Combined sources
Beta strandi108 – 1125Combined sources
Helixi119 – 1246Combined sources
Helixi126 – 1338Combined sources
Helixi135 – 15117Combined sources
Beta strandi156 – 1627Combined sources
Helixi163 – 1664Combined sources
Beta strandi171 – 1733Combined sources
Helixi184 – 20320Combined sources
Beta strandi206 – 2127Combined sources
Helixi225 – 23713Combined sources
Beta strandi244 – 2474Combined sources
Beta strandi252 – 2543Combined sources
Helixi258 – 26912Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi276 – 2794Combined sources
Beta strandi284 – 2863Combined sources
Helixi287 – 29711Combined sources
Helixi302 – 3043Combined sources
Beta strandi306 – 3083Combined sources
Helixi310 – 3123Combined sources
Helixi326 – 3327Combined sources
Helixi340 – 36324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N7GX-ray2.20A/B/C/D1-373[»]
1N7HX-ray1.80A/B1-373[»]
ProteinModelPortaliP93031.
SMRiP93031. Positions 28-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP93031.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni220 – 2289Substrate binding1 Publication
Regioni314 – 3174Substrate binding1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551V → F in AAM61140 (Ref. 5) Curated
Sequence conflicti179 – 1813FHP → IHL in CAB62638 (PubMed:11130713).Curated

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_114976.3.
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_114976.3.
UniGeneiAt.23910.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N7GX-ray2.20A/B/C/D1-373[»]
1N7HX-ray1.80A/B1-373[»]
ProteinModelPortaliP93031.
SMRiP93031. Positions 28-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9598. 3 interactions.
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: September 7, 2016
This is version 121 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.