Skip Header

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

Q93VR3

- GME_ARATH

UniProt

Q93VR3 - GME_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

GDP-mannose 3,5-epimerase

Gene

At5g28840

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

Functioni

Catalyzes a reversible epimerization of GDP-D-mannose that precedes the committed step in the biosynthesis of vitamin C (L-ascorbate), resulting in the hydrolysis of the highly energetic glycosyl-pyrophosphoryl linkage. Able to catalyze 2 distinct epimerization reactions and can release both GDP-L-galactose and GDP-L-gulose from GDP-mannose.1 Publication

Catalytic activityi

GDP-alpha-D-mannose = GDP-beta-L-galactose.2 Publications

Cofactori

NAD(+)1 Publication

Enzyme regulationi

Inhibited by GDP and GDP-D-glucose.1 Publication

Kineticsi

  1. KM=4.5 µM for GDP-mannose1 Publication

Vmax=1.76 µmol/h/mg enzyme with GDP-mannose as substrate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581NAD1 Publication
Binding sitei78 – 781NAD1 Publication
Binding sitei103 – 1031Substrate; via carbonyl oxygen
Active sitei174 – 1741Proton acceptorBy similarity
Binding sitei174 – 1741NAD1 Publication
Binding sitei178 – 1781NAD1 Publication
Binding sitei203 – 2031Substrate
Binding sitei225 – 2251Substrate
Binding sitei306 – 3061Substrate
Binding sitei356 – 3561Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 6027NAD1 PublicationAdd
BLAST

GO - Molecular functioni

  1. GDP-mannose 3,5-epimerase activity Source: TAIR
  2. NAD binding Source: TAIR

GO - Biological processi

  1. L-ascorbic acid biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Ascorbate biosynthesis

Keywords - Ligandi

NAD, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G28840-MONOMER.
ARA:GQT-2356-MONOMER.
MetaCyc:AT5G28840-MONOMER.
SABIO-RKQ93VR3.
UniPathwayiUPA00990; UER00931.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-mannose 3,5-epimerase (EC:5.1.3.18)
Short name:
GDP-Man 3,5-epimerase
Gene namesi
Ordered Locus Names:At5g28840
ORF Names:F7P1.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G28840.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451C → A: Loss of activity. 1 Publication
Mutagenesisi145 – 1451C → S: Strong reduction of activity. 1 Publication
Mutagenesisi174 – 1741Y → F: Loss of activity. 1 Publication
Mutagenesisi178 – 1781K → R: Strong reduction of activity. 1 Publication
Mutagenesisi217 – 2171K → A: Loss of activity. 1 Publication
Mutagenesisi306 – 3061R → A: Strong reduction of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 377376GDP-mannose 3,5-epimerasePRO_0000183267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycine1 Publication
Modified residuei369 – 3691Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ93VR3.
PRIDEiQ93VR3.

Expressioni

Gene expression databases

ExpressionAtlasiQ93VR3. baseline and differential.
GenevestigatoriQ93VR3.

Interactioni

Subunit structurei

Homodimer. Interacts with chaperone Hsc70-3 protein, which may regulate epimerase activity.2 Publications

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 335Combined sources
Turni34 – 363Combined sources
Helixi38 – 4912Combined sources
Beta strandi53 – 608Combined sources
Beta strandi63 – 653Combined sources
Helixi67 – 693Combined sources
Beta strandi72 – 765Combined sources
Helixi82 – 898Combined sources
Beta strandi93 – 975Combined sources
Helixi105 – 1084Combined sources
Helixi112 – 13221Combined sources
Beta strandi136 – 1438Combined sources
Helixi144 – 1463Combined sources
Helixi149 – 1513Combined sources
Beta strandi152 – 1576Combined sources
Helixi162 – 1654Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi170 – 1723Combined sources
Helixi173 – 19220Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi212 – 2143Combined sources
Helixi218 – 22811Combined sources
Beta strandi233 – 2375Combined sources
Beta strandi242 – 2443Combined sources
Helixi248 – 26013Combined sources
Beta strandi267 – 2693Combined sources
Beta strandi274 – 2763Combined sources
Helixi277 – 28610Combined sources
Turni287 – 2893Combined sources
Beta strandi294 – 2974Combined sources
Helixi311 – 3177Combined sources
Helixi325 – 34622Combined sources
Helixi350 – 3545Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C54X-ray1.50A/B1-377[»]
2C59X-ray2.00A/B1-377[»]
2C5AX-ray1.40A/B1-377[»]
2C5EX-ray1.70A/B1-377[»]
ProteinModelPortaliQ93VR3.
SMRiQ93VR3. Positions 13-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ93VR3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni143 – 1453Substrate binding
Regioni216 – 2183Substrate binding
Regioni241 – 2433Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0451.
HOGENOMiHOG000168017.
InParanoidiQ93VR3.
KOiK10046.
OMAiGRNSDNN.
PhylomeDBiQ93VR3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q93VR3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGTTNGTDYG AYTYKELERE QYWPSENLKI SITGAGGFIA SHIARRLKHE
60 70 80 90 100
GHYVIASDWK KNEHMTEDMF CDEFHLVDLR VMENCLKVTE GVDHVFNLAA
110 120 130 140 150
DMGGMGFIQS NHSVIMYNNT MISFNMIEAA RINGIKRFFY ASSACIYPEF
160 170 180 190 200
KQLETTNVSL KESDAWPAEP QDAYGLEKLA TEELCKHYNK DFGIECRIGR
210 220 230 240 250
FHNIYGPFGT WKGGREKAPA AFCRKAQTST DRFEMWGDGL QTRSFTFIDE
260 270 280 290 300
CVEGVLRLTK SDFREPVNIG SDEMVSMNEM AEMVLSFEEK KLPIHHIPGP
310 320 330 340 350
EGVRGRNSDN NLIKEKLGWA PNMRLKEGLR ITYFWIKEQI EKEKAKGSDV
360 370
SLYGSSKVVG TQAPVQLGSL RAADGKE
Length:377
Mass (Da):42,758
Last modified:December 1, 2001 - v1
Checksum:i91C6C4A4C34CCE57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272706 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93843.1.
CP002688 Genomic DNA. Translation: AED93844.1.
AY057660 mRNA. Translation: AAL15291.1.
AY057694 mRNA. Translation: AAL15324.1.
AY116953 mRNA. Translation: AAM51587.1.
RefSeqiNP_001190417.1. NM_001203488.1.
NP_198236.1. NM_122767.3.
UniGeneiAt.21733.

Genome annotation databases

EnsemblPlantsiAT5G28840.1; AT5G28840.1; AT5G28840.
AT5G28840.2; AT5G28840.2; AT5G28840.
GeneIDi833002.
KEGGiath:AT5G28840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF272706 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED93843.1 .
CP002688 Genomic DNA. Translation: AED93844.1 .
AY057660 mRNA. Translation: AAL15291.1 .
AY057694 mRNA. Translation: AAL15324.1 .
AY116953 mRNA. Translation: AAM51587.1 .
RefSeqi NP_001190417.1. NM_001203488.1.
NP_198236.1. NM_122767.3.
UniGenei At.21733.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C54 X-ray 1.50 A/B 1-377 [» ]
2C59 X-ray 2.00 A/B 1-377 [» ]
2C5A X-ray 1.40 A/B 1-377 [» ]
2C5E X-ray 1.70 A/B 1-377 [» ]
ProteinModelPortali Q93VR3.
SMRi Q93VR3. Positions 13-375.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q93VR3.
PRIDEi Q93VR3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G28840.1 ; AT5G28840.1 ; AT5G28840 .
AT5G28840.2 ; AT5G28840.2 ; AT5G28840 .
GeneIDi 833002.
KEGGi ath:AT5G28840.

Organism-specific databases

TAIRi AT5G28840.

Phylogenomic databases

eggNOGi COG0451.
HOGENOMi HOG000168017.
InParanoidi Q93VR3.
KOi K10046.
OMAi GRNSDNN.
PhylomeDBi Q93VR3.

Enzyme and pathway databases

UniPathwayi UPA00990 ; UER00931 .
BioCyci ARA:AT5G28840-MONOMER.
ARA:GQT-2356-MONOMER.
MetaCyc:AT5G28840-MONOMER.
SABIO-RK Q93VR3.

Miscellaneous databases

EvolutionaryTracei Q93VR3.

Gene expression databases

ExpressionAtlasi Q93VR3. baseline and differential.
Genevestigatori Q93VR3.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR001509. Epimerase_deHydtase_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01370. Epimerase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "The biosynthetic pathway of vitamin C in higher plants."
    Wheeler G.L., Jones M.A., Smirnoff N.
    Nature 393:365-369(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PATHWAY.
  5. "Partial purification and identification of GDP-mannose 3',5'-epimerase of Arabidopsis thaliana, a key enzyme of the plant vitamin C pathway."
    Wolucka B.A., Persiau G., Van Doorsselaere J., Davey M.W., Demol H., Vandekerckhove J., Van Montagu M., Zabeau M., Boerjan W.
    Proc. Natl. Acad. Sci. U.S.A. 98:14843-14848(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ENZYME ACTIVITY, COFACTOR, SUBUNIT, INTERACTION WITH HSC70-3.
  6. "GDP-mannose 3',5'-epimerase forms GDP-L-gulose, a putative intermediate for the de novo biosynthesis of vitamin C in plants."
    Wolucka B.A., Van Montagu M.
    J. Biol. Chem. 278:47483-47490(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "Structure and function of GDP-mannose-3',5'-epimerase: an enzyme which performs three chemical reactions at the same active site."
    Major L.L., Wolucka B.A., Naismith J.H.
    J. Am. Chem. Soc. 127:18309-18320(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-377 IN COMPLEX WITH NAD AND SUBSTRATES, SUBUNIT, MUTAGENESIS OF CYS-145; TYR-174; LYS-178; LYS-217 AND ARG-306.

Entry informationi

Entry nameiGME_ARATH
AccessioniPrimary (citable) accession number: Q93VR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 90 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

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

External Data

Dasty 3