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Protein

Mannose-1-phosphate guanylyltransferase 1

Gene

CYT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. Plays an essential role in plant growth and development and cell-wall architecture. Provides GDP-mannose, used for cell wall carbohydrate biosynthesis, protein N-glycosylation, as well as for the biosynthesis of the antioxidant ascorbate.11 Publications

Catalytic activityi

GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.

Pathwayi: GDP-alpha-D-mannose biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route).
Proteins known to be involved in this subpathway in this organism are:
  1. Mannose-1-phosphate guanylyltransferase 1 (CYT1), Probable mannose-1-phosphate guanylyltransferase 2 (At3g55590), Probable mannose-1-phosphate guanylyltransferase 3 (At4g30570)
This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, 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-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route), the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • mannose-1-phosphate guanylyltransferase activity Source: TAIR

GO - Biological processi

  • cellulose biosynthetic process Source: TAIR
  • defense response to bacterium Source: TAIR
  • GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  • L-ascorbic acid biosynthetic process Source: TAIR
  • response to ammonium ion Source: TAIR
  • response to heat Source: TAIR
  • response to jasmonic acid Source: TAIR
  • response to ozone Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:AT2G39770-MONOMER.
BRENDAi2.7.7.13. 399.
UniPathwayiUPA00126; UER00930.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannose-1-phosphate guanylyltransferase 1 (EC:2.7.7.13)
Alternative name(s):
GDP-mannose pyrophosphorylase 1
Protein CYTOKINESIS DEFECTIVE 1
Protein EMBRYO DEFECTIVE 101
Protein HYPERSENSITIVE TO AMMONIUM ION 1
Protein SENSITIVE TO OZONE 1
Protein VITAMIN C DEFECTIVE 1
Gene namesi
Name:CYT1
Synonyms:EMB101, GMP1, HSN1, SOZ1, VTC1
Ordered Locus Names:At2g39770
ORF Names:T5I7.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G39770.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Embryonic lethal. Deficient in N-glycosylation, altered in cytokinesis and cell wall architecture during embryogenesis. Mutants vtc1 and hsn1 with reduced enzyme activity show reduced root length and leaf cell size, reduced accumulation of ascorbate, increased sensitivity to ozone, UV-B and oxidative stresses, increased levels of abscisic acid (ABA), salicylic acid (SA) and resistance to virulent pathogens and root growth inhibition in the presence of NH4+.11 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11G → S in hsn1; reduced enzyme activity, ascorbate concentrations and N-glycosylation, and increased sensitivity to ammonium. 1 Publication1
Mutagenesisi22P → S in vtc1-1 and vtc1-2; reduced enzyme activity and ascorbate concentrations, and ozone-sensitive. 1 Publication1
Mutagenesisi89P → L in cyt1-1; deficient in N-glycosylation and cellulose, and embryo lethal. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004124641 – 361Mannose-1-phosphate guanylyltransferase 1Add BLAST361

Proteomic databases

PaxDbiO22287.
PRIDEiO22287.

Expressioni

Gene expression databases

GenevisibleiO22287. AT.

Interactioni

Protein-protein interaction databases

BioGridi3900. 5 interactors.
IntActiO22287. 2 interactors.
STRINGi3702.AT2G39770.1.

Structurei

3D structure databases

ProteinModelPortaliO22287.
SMRiO22287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1322. Eukaryota.
COG1208. LUCA.
HOGENOMiHOG000283479.
InParanoidiO22287.
KOiK00966.
OMAiWVSLWAG.
OrthoDBiEOG09360CRU.
PhylomeDBiO22287.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001451. Hexapep.
IPR005835. NTP_transferase_dom.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O22287-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALILVGGF GTRLRPLTLS FPKPLVDFAN KPMILHQIEA LKAVGVDEVV
60 70 80 90 100
LAINYQPEVM LNFLKDFETK LEIKITCSQE TEPLGTAGPL ALARDKLLDG
110 120 130 140 150
SGEPFFVLNS DVISEYPLKE MLEFHKSHGG EASIMVTKVD EPSKYGVVVM
160 170 180 190 200
EESTGRVEKF VEKPKLYVGN KINAGIYLLN PSVLDKIELR PTSIEKETFP
210 220 230 240 250
KIAAAQGLYA MVLPGFWMDI GQPRDYITGL RLYLDSLRKK SPAKLTSGPH
260 270 280 290 300
IVGNVLVDET ATIGEGCLIG PDVAIGPGCI VESGVRLSRC TVMRGVRIKK
310 320 330 340 350
HACISSSIIG WHSTVGQWAR IENMTILGED VHVSDEIYSN GGVVLPHKEI
360
KSNILKPEIV M
Length:361
Mass (Da):39,577
Last modified:January 1, 1998 - v1
Checksum:iD282B510E22C2F06
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121M → I in CAC35355 (Ref. 3) Curated1
Sequence conflicti208L → H in CAC35355 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076484 mRNA. Translation: AAC78474.1.
AF108660 mRNA. Translation: AAD04627.1.
AJ275979 Genomic DNA. Translation: CAC35355.1.
AC003000 Genomic DNA. Translation: AAB87126.1.
CP002685 Genomic DNA. Translation: AEC09721.1.
CP002685 Genomic DNA. Translation: AEC09722.1.
AF361812 mRNA. Translation: AAK32825.1.
AY057541 mRNA. Translation: AAL09781.1.
AF428297 mRNA. Translation: AAL16129.1.
AY133643 mRNA. Translation: AAM91473.1.
BT000697 mRNA. Translation: AAN31841.1.
BT006365 mRNA. Translation: AAP21173.1.
AY087698 mRNA. Translation: AAM65235.1.
PIRiT01007.
RefSeqiNP_001189713.1. NM_001202784.1.
NP_181507.1. NM_129535.4.
UniGeneiAt.10348.

Genome annotation databases

EnsemblPlantsiAT2G39770.1; AT2G39770.1; AT2G39770.
AT2G39770.2; AT2G39770.2; AT2G39770.
GeneIDi818562.
GrameneiAT2G39770.1; AT2G39770.1; AT2G39770.
AT2G39770.2; AT2G39770.2; AT2G39770.
KEGGiath:AT2G39770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076484 mRNA. Translation: AAC78474.1.
AF108660 mRNA. Translation: AAD04627.1.
AJ275979 Genomic DNA. Translation: CAC35355.1.
AC003000 Genomic DNA. Translation: AAB87126.1.
CP002685 Genomic DNA. Translation: AEC09721.1.
CP002685 Genomic DNA. Translation: AEC09722.1.
AF361812 mRNA. Translation: AAK32825.1.
AY057541 mRNA. Translation: AAL09781.1.
AF428297 mRNA. Translation: AAL16129.1.
AY133643 mRNA. Translation: AAM91473.1.
BT000697 mRNA. Translation: AAN31841.1.
BT006365 mRNA. Translation: AAP21173.1.
AY087698 mRNA. Translation: AAM65235.1.
PIRiT01007.
RefSeqiNP_001189713.1. NM_001202784.1.
NP_181507.1. NM_129535.4.
UniGeneiAt.10348.

3D structure databases

ProteinModelPortaliO22287.
SMRiO22287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3900. 5 interactors.
IntActiO22287. 2 interactors.
STRINGi3702.AT2G39770.1.

Proteomic databases

PaxDbiO22287.
PRIDEiO22287.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G39770.1; AT2G39770.1; AT2G39770.
AT2G39770.2; AT2G39770.2; AT2G39770.
GeneIDi818562.
GrameneiAT2G39770.1; AT2G39770.1; AT2G39770.
AT2G39770.2; AT2G39770.2; AT2G39770.
KEGGiath:AT2G39770.

Organism-specific databases

TAIRiAT2G39770.

Phylogenomic databases

eggNOGiKOG1322. Eukaryota.
COG1208. LUCA.
HOGENOMiHOG000283479.
InParanoidiO22287.
KOiK00966.
OMAiWVSLWAG.
OrthoDBiEOG09360CRU.
PhylomeDBiO22287.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00930.
BioCyciMetaCyc:AT2G39770-MONOMER.
BRENDAi2.7.7.13. 399.

Miscellaneous databases

PROiO22287.

Gene expression databases

GenevisibleiO22287. AT.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001451. Hexapep.
IPR005835. NTP_transferase_dom.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00132. Hexapep. 1 hit.
PF00483. NTP_transferase. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00101. HEXAPEP_TRANSFERASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGMPP1_ARATH
AccessioniPrimary (citable) accession number: O22287
Secondary accession number(s): Q9C5B8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.