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Protein

Alpha-glucan water dikinase 2

Gene

GWD2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates the incorporation of phosphate into alpha-glucan, mostly at the C-6 position of glucose units.By similarity

Catalytic activityi

ATP + alpha-glucan + H2O = AMP + phospho-alpha-glucan + phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei886 – 8861Tele-phosphohistidine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G24450-MONOMER.
BRENDAi2.7.9.4. 399.

Protein family/group databases

CAZyiCBM45. Carbohydrate-Binding Module Family 45.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucan water dikinase 2 (EC:2.7.9.4)
Gene namesi
Name:GWD2
Ordered Locus Names:At4g24450
ORF Names:T22A6.280
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G24450.

Subcellular locationi

GO - Cellular componenti

  • chloroplast envelope Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 12781255Alpha-glucan water dikinase 2PRO_0000240249Add
BLAST

Proteomic databases

PaxDbiQ9STV0.
PRIDEiQ9STV0.

Expressioni

Gene expression databases

GenevisibleiQ9STV0. AT.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi3702.AT4G24450.1.

Structurei

3D structure databases

ProteinModelPortaliQ9STV0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal domain contains the alpha-glucan binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the ATP binding site.By similarity

Sequence similaritiesi

Belongs to the PEP-utilizing enzyme family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHGM. Eukaryota.
ENOG410XUE8. LUCA.
HOGENOMiHOG000265165.
InParanoidiQ9STV0.
KOiK08244.
OMAiHVSIRAR.

Family and domain databases

Gene3Di3.30.1490.20. 2 hits.
3.30.470.20. 1 hit.
InterProiIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR002192. PPDK_PEP-bd.
[Graphical view]
PfamiPF01326. PPDK_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9STV0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSKSQQFQ LIEGMELQIT VTGLPNGSSV RAEFHLKNCT RAWILHWGCI
60 70 80 90 100
YQGNNHWYIP SEHSSKQGAL QTTFVKSGDA YVVILELRDP RVRAIEFVLK
110 120 130 140 150
DGSHNRWLRQ HNGNFRVEIP WNDLHAHHRI PKTLIERRAH KIWDRKGRPQ
160 170 180 190 200
SSAREQQIDY DNAVRELHAE LARGISLDEL QANSTVPVEK EETSEPHHTM
210 220 230 240 250
IQSYRRKHDV QKWLQKYTEP INRSGSVKSS ALAELSKRSV GQENLVSQKS
260 270 280 290 300
FHVRNYEITV LQRDVKGDCR LWIATNMAGP TVLHWGVAKS SAGEWLIPPP
310 320 330 340 350
DVLPEKSKFV HGACQTQFTD MSSREHSYQF IDINLKRGGF VGIQFVIWSG
360 370 380 390 400
GYWVNNNGAN FVVNLKSADS TSGKLDVDEK YVLKWLLDEI SEREKEAERS
410 420 430 440 450
LMHRFNIATE LTERCKDEGE GGCIGIMVWM RFMATRHLTW NKNYNVKPRE
460 470 480 490 500
ISEALERFTN LMEKIYLQQP NKREIVRLTM ALVGRGGQGD VGQRIRDEIL
510 520 530 540 550
VIQRNNHCKS GMMEEWHQKL HNNSSADDVI ICEALLNYVR SDFRIDAYWQ
560 570 580 590 600
TLQTNGLTKE RLASYDRPIV SEPRFRSDSK EGLIRDLTMY LKTLKAVHSG
610 620 630 640 650
ADLESAIDTF LSPSKGHHVF AVNGLSPKLQ DLLNLVKRLV REENTEPLIE
660 670 680 690 700
KLVDARIQLH PALRAPRTRA KDLLFLDIAL ESCFKTTIEK RLISLNFNNP
710 720 730 740 750
PEIIYVICVV LENLCLSIVN NEEIIFCTKD WYRVSEAYRP HDVQWALQTK
760 770 780 790 800
AVLDRLQLVL ADRCQHYFTI IQPTAKYLGQ LLRVDKHGID VFTEEVIRAG
810 820 830 840 850
PGAVLSTLVN RFDPSLRKIA NLGCWQVISS ADAYGFVVCV NELIVVQNKF
860 870 880 890 900
YSKPTVIIAS KVTGEEEIPA GVVAVLTPSM IDVLSHVSIR ARNSKICFAT
910 920 930 940 950
CFDQNVLSNL KSKEGRAISI HTKSTGLVIS DGNNSDVSVR HIFISSVPRG
960 970 980 990 1000
VISKGKKFCG HYVISSKEFT DERVGSKSYN IKFLRERVPS WIKIPTSAAL
1010 1020 1030 1040 1050
PFGTFENILS DDSNKDVARR ISVLKDSLNR GDLTKLKSIQ EAILQMSAPM
1060 1070 1080 1090 1100
ALRNELITKL RSERMPYLGD ESGWNRSWVA IKKVWASKWN ERAYVSCKKN
1110 1120 1130 1140 1150
KLDHDAVCMA VLIQEVICGD YAFVIHTNNP VSGDSSEIYT EIVKGLGETL
1160 1170 1180 1190 1200
VGAYPGRAMS FITKKTNLKS PTVISYPSKR IGLYSKPSII FRSDSNNEDL
1210 1220 1230 1240 1250
EGNAGAGLYD SVIMDEAEEV VVDYSREPLI MDKSFRVRLF SAIAEAGNVI
1260 1270
ESIYGCPQDI EGVVKGGHIY IVQARPQV
Length:1,278
Mass (Da):144,812
Last modified:May 3, 2011 - v3
Checksum:iC62746575CFCFA00
GO

Sequence cautioni

The sequence CAB45080.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79355.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031S → N in AAO42141 (PubMed:14593172).Curated
Sequence conflicti254 – 2541R → G in AAO42141 (PubMed:14593172).Curated
Sequence conflicti630 – 6301Q → R in AAO42141 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078637 Genomic DNA. Translation: CAB45080.1. Sequence problems.
AL161561 Genomic DNA. Translation: CAB79355.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84906.1.
BT004118 mRNA. Translation: AAO42141.1.
PIRiT09908.
RefSeqiNP_194176.3. NM_118578.4.
UniGeneiAt.46227.

Genome annotation databases

EnsemblPlantsiAT4G24450.1; AT4G24450.1; AT4G24450.
GeneIDi828547.
GrameneiAT4G24450.1; AT4G24450.1; AT4G24450.
KEGGiath:AT4G24450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL078637 Genomic DNA. Translation: CAB45080.1. Sequence problems.
AL161561 Genomic DNA. Translation: CAB79355.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84906.1.
BT004118 mRNA. Translation: AAO42141.1.
PIRiT09908.
RefSeqiNP_194176.3. NM_118578.4.
UniGeneiAt.46227.

3D structure databases

ProteinModelPortaliQ9STV0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G24450.1.

Protein family/group databases

CAZyiCBM45. Carbohydrate-Binding Module Family 45.

Proteomic databases

PaxDbiQ9STV0.
PRIDEiQ9STV0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G24450.1; AT4G24450.1; AT4G24450.
GeneIDi828547.
GrameneiAT4G24450.1; AT4G24450.1; AT4G24450.
KEGGiath:AT4G24450.

Organism-specific databases

TAIRiAT4G24450.

Phylogenomic databases

eggNOGiENOG410IHGM. Eukaryota.
ENOG410XUE8. LUCA.
HOGENOMiHOG000265165.
InParanoidiQ9STV0.
KOiK08244.
OMAiHVSIRAR.

Enzyme and pathway databases

BioCyciARA:AT4G24450-MONOMER.
BRENDAi2.7.9.4. 399.

Miscellaneous databases

PROiQ9STV0.

Gene expression databases

GenevisibleiQ9STV0. AT.

Family and domain databases

Gene3Di3.30.1490.20. 2 hits.
3.30.470.20. 1 hit.
InterProiIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR002192. PPDK_PEP-bd.
[Graphical view]
PfamiPF01326. PPDK_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [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.

Entry informationi

Entry nameiGWD2_ARATH
AccessioniPrimary (citable) accession number: Q9STV0
Secondary accession number(s): Q84W86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: May 3, 2011
Last modified: June 8, 2016
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the C-terminal domain, and the third partial reaction is catalyzed at an active site located on the N-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the C-terminal domain to that of the B-terminal domain (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.