Reviewed, UniProtKB/Swiss-Prot Q9STV0 (GWD2_ARATH)

Names and origin

Protein names

Recommended name:
    Alpha-glucan water dikinase 2
    EC=2.7.9.4

Gene names

Name:	GWD2
Ordered Locus Names:	At4g24450
ORF Names:	T22A6.280

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	1278 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Mediates the incorporation of phosphate into alpha-glucan, mostly at the C-6 position of glucose units By similarity.
Catalytic activity	ATP + alpha-glucan + H2O = AMP + phospho-alpha-glucan + phosphate.
Cofactor	Magnesium By similarity.
Subunit structure	Homodimer By similarity.
Domain	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.
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.
Sequence similarities	Belongs to the PEP-utilizing enzyme family.
Sequence caution	The sequence CAB45080.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB79355.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Signal
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alpha-glucan, water dikinase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 1278	1255	Alpha-glucan water dikinase 2		PRO_0000240249
Sites
	Active site	886	1	Tele-phosphohistidine intermediate By similarity
Experimental info
	Sequence conflict	103	1	S → N in AAO42141. Ref.2
	Sequence conflict	254	1	R → G in AAO42141. Ref.2
	Sequence conflict	630	1	Q → R in AAO42141. Ref.2
	Sequence conflict	896	1	A → I in AAO42141. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9STV0-1 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: 198F450CD80F7B73	FASTA	1,278	144,770
	10 20 30 40 50 60 MATSKSQQFQ LIEGMELQIT VTGLPNGSSV RAEFHLKNCT RAWILHWGCI YQGNNHWYIP 70 80 90 100 110 120 SEHSSKQGAL QTTFVKSGDA YVVILELRDP RVRAIEFVLK DGSHNRWLRQ HNGNFRVEIP 130 140 150 160 170 180 WNDLHAHHRI PKTLIERRAH KIWDRKGRPQ SSAREQQIDY DNAVRELHAE LARGISLDEL 190 200 210 220 230 240 QANSTVPVEK EETSEPHHTM IQSYRRKHDV QKWLQKYTEP INRSGSVKSS ALAELSKRSV 250 260 270 280 290 300 GQENLVSQKS FHVRNYEITV LQRDVKGDCR LWIATNMAGP TVLHWGVAKS SAGEWLIPPP 310 320 330 340 350 360 DVLPEKSKFV HGACQTQFTD MSSREHSYQF IDINLKRGGF VGIQFVIWSG GYWVNNNGAN 370 380 390 400 410 420 FVVNLKSADS TSGKLDVDEK YVLKWLLDEI SEREKEAERS LMHRFNIATE LTERCKDEGE 430 440 450 460 470 480 GGCIGIMVWM RFMATRHLTW NKNYNVKPRE ISEALERFTN LMEKIYLQQP NKREIVRLTM 490 500 510 520 530 540 ALVGRGGQGD VGQRIRDEIL VIQRNNHCKS GMMEEWHQKL HNNSSADDVI ICEALLNYVR 550 560 570 580 590 600 SDFRIDAYWQ TLQTNGLTKE RLASYDRPIV SEPRFRSDSK EGLIRDLTMY LKTLKAVHSG 610 620 630 640 650 660 ADLESAIDTF LSPSKGHHVF AVNGLSPKLQ DLLNLVKRLV REENTEPLIE KLVDARIQLH 670 680 690 700 710 720 PALRAPRTRA KDLLFLDIAL ESCFKTTIEK RLISLNFNNP PEIIYVICVV LENLCLSIVN 730 740 750 760 770 780 NEEIIFCTKD WYRVSEAYRP HDVQWALQTK AVLDRLQLVL ADRCQHYFTI IQPTAKYLGQ 790 800 810 820 830 840 LLRVDKHGID VFTEEVIRAG PGAVLSTLVN RFDPSLRKIA NLGCWQVISS ADAYGFVVCV 850 860 870 880 890 900 NELIVVQNKF YSKPTVIIAS KVTGEEEIPA GVVAVLTPSM IDVLSHVSIR ARNSKACFAT 910 920 930 940 950 960 CFDQNVLSNL KSKEGRAISI HTKSTGLVIS DGNNSDVSVR HIFISSVPRG VISKGKKFCG 970 980 990 1000 1010 1020 HYVISSKEFT DERVGSKSYN IKFLRERVPS WIKIPTSAAL PFGTFENILS DDSNKDVARR 1030 1040 1050 1060 1070 1080 ISVLKDSLNR GDLTKLKSIQ EAILQMSAPM ALRNELITKL RSERMPYLGD ESGWNRSWVA 1090 1100 1110 1120 1130 1140 IKKVWASKWN ERAYVSCKKN KLDHDAVCMA VLIQEVICGD YAFVIHTNNP VSGDSSEIYT 1150 1160 1170 1180 1190 1200 EIVKGLGETL VGAYPGRAMS FITKKTNLKS PTVISYPSKR IGLYSKPSII FRSDSNNEDL 1210 1220 1230 1240 1250 1260 EGNAGAGLYD SVIMDEAEEV VVDYSREPLI MDKSFRVRLF SAIAEAGNVI ESIYGCPQDI 1270 EGVVKGGHIY IVQARPQV

References

[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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.

[2]

"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL078637 Genomic DNA. Translation: CAB45080.1. Sequence problems. AL161561 Genomic DNA. Translation: CAB79355.1. Sequence problems. BT004118 mRNA. Translation: AAO42141.1.
IPI	IPI00519448.
PIR	T09908.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	CBM45. Carbohydrate-Binding Module Family 45.
Genome annotation databases
GenomeReviews	Gene locus AT4G24450 in contig CT486007_GR.
Organism-specific databases
TAIR	At4g24450.
Enzyme and pathway databases
BRENDA	2.7.9.4. 302.
Gene expression databases
GermOnline	AT4G24450. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR018274. PEP_mobile_CS. IPR000121. PEP_utilizers. IPR002192. PPDK_PEP_bd. [Graphical view]
Pfam	PF01326. PPDK_N. 2 hits. [Graphical view]
PROSITE	PS00742. PEP_ENZYMES_2. False negative. PS00370. PEP_ENZYMES_PHOS_SITE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GWD2_ARATH

Accession

Primary (citable) accession number: Q9STV0
Secondary accession number(s): Q84W86

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	June 13, 2006
Last modified:	June 16, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)