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Q43846

- SSY3_SOLTU

UniProt

Q43846 - SSY3_SOLTU

Protein

Soluble starch synthase 3, chloroplastic/amyloplastic

Gene

SS3

Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    May account for most of the soluble starch synthase activity in the tubers. Contributes only a tiny percentage of the granule-bound activity, but may also contribute to the deposition of transient starch in chloroplasts of leaves.

    Catalytic activityi

    ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1).

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei794 – 7941ADP-glucoseBy similarity

    GO - Molecular functioni

    1. starch binding Source: InterPro
    2. starch synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. starch biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Starch biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-1884.
    UniPathwayiUPA00152.

    Protein family/group databases

    CAZyiCBM53. Carbohydrate-Binding Module Family 53.
    GT5. Glycosyltransferase Family 5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Soluble starch synthase 3, chloroplastic/amyloplastic (EC:2.4.1.21)
    Alternative name(s):
    Soluble starch synthase III
    Short name:
    SS III
    Gene namesi
    Name:SS3
    Synonyms:SSIII
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: Unplaced

    Subcellular locationi

    Plastidchloroplast By similarity. Plastidamyloplast By similarity
    Note: Amyloplast or chloroplast, granule-bound and soluble.By similarity

    GO - Cellular componenti

    1. amyloplast Source: UniProtKB-SubCell
    2. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Amyloplast, Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6060ChloroplastSequence AnalysisAdd
    BLAST
    Chaini61 – 12301170Soluble starch synthase 3, chloroplastic/amyloplasticPRO_0000011146Add
    BLAST

    Expressioni

    Tissue specificityi

    Tuber, sink and source leaves.

    Inductioni

    By sucrose under illumination.

    Structurei

    3D structure databases

    ProteinModelPortaliQ43846.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    HAMAPiMF_00484. Glycogen_synth.
    InterProiIPR005085. CBM_fam25.
    IPR001296. Glyco_trans_1.
    IPR011835. Glycogen/starch_synth.
    IPR013534. Starch_synth_cat_dom.
    [Graphical view]
    PfamiPF03423. CBM_25. 3 hits.
    PF08323. Glyco_transf_5. 1 hit.
    PF00534. Glycos_transf_1. 1 hit.
    [Graphical view]
    SMARTiSM01066. CBM_25. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q43846-1 [UniParc]FASTAAdd to Basket

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    MDVPFPLHRS LSCTSVSNAI THLKIKPILG FVSHGTTSLS VQSSSWRKDG     50
    MVTGVSFSIC ANFSGRRRRK VSTPRSQGSS PKGFVPRKPS GMSTQRKVQK 100
    SNGDKESKST STSKESEISN QKTVEARVET SDDDTKGVVR DHKFLEDEDE 150
    INGSTKSISM SPVRVSSQFV ESEETGGDDK DAVKLNKSKR SEESGFIIDS 200
    VIREQSGSQG ETNASSKGSH AVGTKLYEIL QVDVEPQQLK ENNAGNVEYK 250
    GPVASKLLEI TKASDVEHTE SNEIDDLDTN SFFKSDLIEE DEPLAAGTVE 300
    TGDSSLNLRL EMEANLRRQA IERLAEENLL QGIRLFCFPE VVKPDEDVEI 350
    FLNRGLSTLK NESDVLIMGA FNEWRYRSFT TRLTETHLNG DWWSCKIHVP 400
    KEAYRADFVF FNGQDVYDNN DGNDFSITVK GGMQIIDFEN FLLEEKWREQ 450
    EKLAKEQAER ERLAEEQRRI EAEKAEIEAD RAQAKEEAAK KKKVLRELMV 500
    KATKTRDITW YIEPSEFKCE DKVRLYYNKS SGPLSHAKDL WIHGGYNNWK 550
    DGLSIVKKLV KSERIDGDWW YTEVVIPDQA LFLDWVFADG PPKHAIAYDN 600
    NHRQDFHAIV PNHIPEELYW VEEEHQIFKT LQEERRLREA AMRAKVEKTA 650
    LLKTETKERT MKSFLLSQKH VVYTEPLDIQ AGSSVTVYYN PANTVLNGKP 700
    EIWFRCSFNR WTHRLGPLPP QKMSPAENGT HVRATVKVPL DAYMMDFVFS 750
    EREDGGIFDN KSGMDYHIPV FGGVAKEPPM HIVHIAVEMA PIAKVGGLGD 800
    VVTSLSRAVQ DLNHNVDIIL PKYDCLKMNN VKDFRFHKNY FWGGTEIKVW 850
    FGKVEGLSVY FLEPQNGLFS KGCVYGCSND GERFGFFCHA ALEFLLQGGF 900
    SPDIIHCHDW SSAPVAWLFK EQYTHYGLSK SRIVFTIHNL EFGADLIGRA 950
    MTNADKATTV SPTYSQEVSG NPVIAPHLHK FHGIVNGIDP DIWDPLNDKF 1000
    IPIPYTSENV VEGKTAAKEA LQRKLGLKQA DLPLVGIITR LTHQKGIHLI 1050
    KHAIWRTLER NGQVVLLGSA PDPRVQNNFV NLANQLHSKY NDRARLCLTY 1100
    DEPLSHLIYA GADFILVPSI FEPCGLTQLT AMRYGSIPVV RKTGGLYDTV 1150
    FDVDHDKERA QQCGLEPNGF SFDGADAGGV DYALNRALSA WYDGRDWFNS 1200
    LCKQVMEQDW SWNRPALDYL ELYHAARKLE 1230
    Length:1,230
    Mass (Da):139,111
    Last modified:November 1, 1996 - v1
    Checksum:i3D95524F3DD9349E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101S → P in CAA64173. (PubMed:9011082)Curated
    Sequence conflicti28 – 281I → F in CAA64173. (PubMed:9011082)Curated
    Sequence conflicti58 – 592SI → PF in CAA64173. (PubMed:9011082)Curated
    Sequence conflicti63 – 631F → L in CAA64173. (PubMed:9011082)Curated
    Sequence conflicti74 – 741P → T in CAA64173. (PubMed:9011082)Curated
    Sequence conflicti108 – 1081K → Q in CAA64173. (PubMed:9011082)Curated
    Sequence conflicti137 – 1371G → V in CAA64173. (PubMed:9011082)Curated
    Sequence conflicti195 – 1951G → D(PubMed:9011082)Curated
    Sequence conflicti197 – 1971I → L(PubMed:9011082)Curated
    Sequence conflicti1078 – 10781N → D in CAA64173. (PubMed:9011082)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95759 mRNA. Translation: CAA65065.1.
    X94400 mRNA. Translation: CAA64173.1.
    PIRiT07663.
    UniGeneiStu.198.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95759 mRNA. Translation: CAA65065.1 .
    X94400 mRNA. Translation: CAA64173.1 .
    PIRi T07663.
    UniGenei Stu.198.

    3D structure databases

    ProteinModelPortali Q43846.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM53. Carbohydrate-Binding Module Family 53.
    GT5. Glycosyltransferase Family 5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00152 .
    BioCyci MetaCyc:MONOMER-1884.

    Family and domain databases

    HAMAPi MF_00484. Glycogen_synth.
    InterProi IPR005085. CBM_fam25.
    IPR001296. Glyco_trans_1.
    IPR011835. Glycogen/starch_synth.
    IPR013534. Starch_synth_cat_dom.
    [Graphical view ]
    Pfami PF03423. CBM_25. 3 hits.
    PF08323. Glyco_transf_5. 1 hit.
    PF00534. Glycos_transf_1. 1 hit.
    [Graphical view ]
    SMARTi SM01066. CBM_25. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the major starch synthase in the soluble fraction of potato tubers."
      Marshall J., Sidebottom C., Debet M., Martin C., Smith A.M., Edwards A.
      Plant Cell 8:1121-1135(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 767-773 AND 1000-1014.
      Strain: cv. Desiree.
      Tissue: Tuber.
    2. "Cloning and functional analysis of a cDNA encoding a novel 139 kDa starch synthase from potato (Solanum tuberosum L.)."
      Abel G.J.W., Springer F., Willmitzer L., Kossmann J.
      Plant J. 10:981-991(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Desiree.

    Entry informationi

    Entry nameiSSY3_SOLTU
    AccessioniPrimary (citable) accession number: Q43846
    Secondary accession number(s): O04842
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 82 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, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3