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Q9SAC6 (GWD1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-glucan water dikinase 1, chloroplastic

EC=2.7.9.4
Alternative name(s):
Protein starch excess 1
Protein starch-related R1
Gene names
Name:GWD1
Synonyms:R1, SEX1
Ordered Locus Names:At1g10760
ORF Names:F20B24.19, T16B5.10
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the incorporation of phosphate into starch-like alpha-glucan, mostly at the C-6 position of glucose units. Acts as an overall regulator of starch mobilization. Required for starch degradation, suggesting that the phosphate content of starch regulates its degradability. Ref.1

Catalytic activity

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

Cofactor

Magnesium By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastidchloroplast. Note: Starch granules. Ref.1

Developmental stage

The level of protein does not vary in a circadian rhythm and is stable throughout day and night (at protein level). Ref.1

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 N-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Sequence caution

The sequence AAD31337.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAF17665.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAK49609.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAK96541.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7575Chloroplast By similarity
Chain76 – 13991324Alpha-glucan water dikinase 1, chloroplastic
PRO_0000023565

Sites

Active site10041Tele-phosphohistidine intermediate By similarity

Experimental info

Mutagenesis12681G → E in sex1-1; induces an excess of starch in leaves after a long period of darkness. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9SAC6 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 1FE9285376B479EB

FASTA1,399156,582
        10         20         30         40         50         60 
MSNSVVHNLL NRGLIRPLNF EHQNKLNSSV YQTSTANPAL GKIGRSKLYG KGLKQAGRSL 

        70         80         90        100        110        120 
VTETGGRPLS FVPRAVLAMD PQAAEKFSLD GNIDLLVEVT STTVREVNIQ IAYTSDTLFL 

       130        140        150        160        170        180 
HWGAILDNKE NWVLPSRSPD RTQNFKNSAL RTPFVKSGGN SHLKLEIDDP AIHAIEFLIF 

       190        200        210        220        230        240 
DESRNKWYKN NGQNFHINLP TERNVKQNVS VPEDLVQIQA YLRWERKGKQ MYNPEKEKEE 

       250        260        270        280        290        300 
YEAARTELRE EMMRGASVED LRAKLLKKDN SNESPKSNGT SSSGREEKKK VSKQPERKKN 

       310        320        330        340        350        360 
YNTDKIQRKG RDLTKLIYKH VADFVEPESK SSSEPRSLTT LEIYAKAKEE QETTPVFSKK 

       370        380        390        400        410        420 
TFKLEGSAIL VFVTKLSGKT KIHVATDFKE PVTLHWALSQ KGGEWLDPPS DILPPNSLPV 

       430        440        450        460        470        480 
RGAVDTKLTI TSTDLPSPVQ TFELEIEGDS YKGMPFVLNA GERWIKNNDS DFYVDFAKEE 

       490        500        510        520        530        540 
KHVQKDYGDG KGTAKHLLDK IADLESEAQK SFMHRFNIAA DLVDEAKSAG QLGFAGILVW 

       550        560        570        580        590        600 
MRFMATRQLV WNKNYNVKPR EISKAQDRLT DLLQDVYASY PEYRELLRMI MSTVGRGGEG 

       610        620        630        640        650        660 
DVGQRIRDEI LVIQRKNDCK GGIMEEWHQK LHNNTSPDDV VICQALMDYI KSDFDLSVYW 

       670        680        690        700        710        720 
KTLNDNGITK ERLLSYDRAI HSEPNFRGEQ KDGLLRDLGH YMRTLKAVHS GADLESAIQN 

       730        740        750        760        770        780 
CMGYQDDGEG FMVGVQINPV SGLPSGYPDL LRFVLEHVEE KNVEPLLEGL LEARQELRPL 

       790        800        810        820        830        840 
LLKSHDRLKD LLFLDLALDS TVRTAIERGY EQLNDAGPEK IMYFISLVLE NLALSSDDNE 

       850        860        870        880        890        900 
DLIYCLKGWQ FALDMCKSKK DHWALYAKSV LDRSRLALAS KAERYLEILQ PSAEYLGSCL 

       910        920        930        940        950        960 
GVDQSAVSIF TEEIIRAGSA AALSSLVNRL DPVLRKTANL GSWQVISPVE VVGYVIVVDE 

       970        980        990       1000       1010       1020 
LLTVQNKTYD RPTIIVANRV RGEEEIPDGA VAVLTPDMPD VLSHVSVRAR NGKICFATCF 

      1030       1040       1050       1060       1070       1080 
DSGILSDLQG KDGKLLSLQP TSADVVYKEV NDSELSSPSS DNLEDAPPSI SLVKKQFAGR 

      1090       1100       1110       1120       1130       1140 
YAISSEEFTS DLVGAKSRNI GYLKGKVPSW VGIPTSVALP FGVFEKVISE KANQAVNDKL 

      1150       1160       1170       1180       1190       1200 
LVLKKTLDEG DQGALKEIRQ TLLGLVAPPE LVEELKSTMK SSDMPWPGDE GEQRWEQAWA 

      1210       1220       1230       1240       1250       1260 
AIKKVWASKW NERAYFSTRK VKLDHDYLCM AVLVQEVINA DYAFVIHTTN PSSGDSSEIY 

      1270       1280       1290       1300       1310       1320 
AEVVKGLGET LVGAYPGRSL SFICKKNNLD SPLVLGYPSK PIGLFIRRSI IFRSDSNGED 

      1330       1340       1350       1360       1370       1380 
LEGYAGAGLY DSVPMDEEDQ VVLDYTTDPL ITDLSFQKKV LSDIARAGDA IEKLYGTAQD 

      1390 
IEGVIRDGKL YVVQTRPQV 

« Hide

References

« Hide 'large scale' references
[1]"The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter."
Yu T.-S., Kofler H., Haeusler R.E., Hille D., Fluegge U.-I., Zeeman S.C., Smith A.M., Kossmann J., Lloyd J., Ritte G., Steup M., Lue W.-L., Chen J., Weber A.
Plant Cell 13:1907-1918(2001) [PubMed: 11487701] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLY-1268.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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] OF 1220-1399.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312027 mRNA. Translation: AAG47821.1.
AC007354 Genomic DNA. Translation: AAD31337.1. Sequence problems.
AC009398 Genomic DNA. Translation: AAF17665.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28643.1.
AF372893 mRNA. Translation: AAK49609.1. Different initiation.
AY052349 mRNA. Translation: AAK96541.1. Different initiation.
AY057722 mRNA. Translation: AAL15352.1.
IPIIPI00521332.
PIRB86241.
RefSeqNP_563877.1. NM_100952.4.
UniGeneAt.22136.

3D structure databases

ProteinModelPortalQ9SAC6.
SMRQ9SAC6. Positions 1080-1399.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9SAC6. 1 interaction.
STRINGQ9SAC6.

Protein family/group databases

CAZyCBM45. Carbohydrate-Binding Module Family 45.

Proteomic databases

PRIDEQ9SAC6.
ProMEXQ9SAC6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G10760.1; AT1G10760.1; AT1G10760.
GeneID837619.
GenomeReviewsGene locus AT1G10760 in contig CT485782_GR.
KEGGath:AT1G10760.
NMPDRfig|3702.1.peg.1325.

Organism-specific databases

TAIRAt1g10760.

Phylogenomic databases

GeneTreeEPGT00070000029920.
HOGENOMHBG561530.
InParanoidQ9SAC6.
OMAKIMYFIS.
PhylomeDBQ9SAC6.
ProtClustDBCLSN2687761.

Enzyme and pathway databases

BioCycARA:AT1G10760-MONOMER.
MetaCyc:AT1G10760-MONOMER.

Gene expression databases

ArrayExpressQ9SAC6.
GenevestigatorQ9SAC6.
GermOnlineAT1G10760. Arabidopsis thaliana.

Family and domain databases

InterProIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR002192. PPDK_PEP-bd.
[Graphical view]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 2 hits.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits.
KOK08244.
PfamPF01326. PPDK_N. 1 hit.
[Graphical view]
PROSITEPS00742. PEP_ENZYMES_2. False negative.
PS00370. PEP_ENZYMES_PHOS_SITE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGWD1_ARATH
AccessionPrimary (citable) accession number: Q9SAC6
Secondary accession number(s): Q93VD0 expand/collapse secondary AC list , Q940Z0, Q9FPP2, Q9SGX4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: December 14, 2011
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families