Soluble starch synthase 3, chloroplastic/amyloplastic precursor

Preferred order of sections

Names and origin

Protein names

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 names

Name:	SS3
Synonyms:	SSIII

Organism

Solanum tuberosum (Potato) [Reference proteome]

Taxonomic identifier

4113 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length	1230 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP + (1,4-alpha-D-glucosyl)(n+1).
Pathway	Glycan biosynthesis; starch biosynthesis.
Subcellular location	Plastid › chloroplast By similarity. Plastid › amyloplast By similarity. Note: Amyloplast or chloroplast, granule-bound and soluble By similarity.
Tissue specificity	Tuber, sink and source leaves.
Induction	By sucrose under illumination.
Sequence similarities	Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.

Ontologies

Keywords
Biological process	Starch biosynthesis
Cellular component	Amyloplast Chloroplast Plastid
Domain	Transit peptide
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	starch biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	starch binding Inferred from electronic annotation. Source: InterPro starch synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 60

60

Chloroplast Potential

Chain

61 – 1230

1170

Soluble starch synthase 3, chloroplastic/amyloplastic

PRO_0000011146

Sites

Binding site

794

1

ADP-glucose By similarity

Experimental info

Sequence conflict

10

1

S → P in CAA64173. Ref.2

Sequence conflict

28

1

I → F in CAA64173. Ref.2

Sequence conflict

58 – 59

2

SI → PF in CAA64173. Ref.2

Sequence conflict

63

1

F → L in CAA64173. Ref.2

Sequence conflict

74

1

P → T in CAA64173. Ref.2

Sequence conflict

108

1

K → Q in CAA64173. Ref.2

Sequence conflict

137

1

G → V in CAA64173. Ref.2

Sequence conflict

195

1

G → D Ref.2

Sequence conflict

197

1

I → L Ref.2

Sequence conflict

1078

1

N → D in CAA64173. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q43846 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3D95524F3DD9349E
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FASTA

1,230

139,111

        10         20         30         40         50         60 
MDVPFPLHRS LSCTSVSNAI THLKIKPILG FVSHGTTSLS VQSSSWRKDG MVTGVSFSIC 

        70         80         90        100        110        120 
ANFSGRRRRK VSTPRSQGSS PKGFVPRKPS GMSTQRKVQK SNGDKESKST STSKESEISN 

       130        140        150        160        170        180 
QKTVEARVET SDDDTKGVVR DHKFLEDEDE INGSTKSISM SPVRVSSQFV ESEETGGDDK 

       190        200        210        220        230        240 
DAVKLNKSKR SEESGFIIDS VIREQSGSQG ETNASSKGSH AVGTKLYEIL QVDVEPQQLK 

       250        260        270        280        290        300 
ENNAGNVEYK GPVASKLLEI TKASDVEHTE SNEIDDLDTN SFFKSDLIEE DEPLAAGTVE 

       310        320        330        340        350        360 
TGDSSLNLRL EMEANLRRQA IERLAEENLL QGIRLFCFPE VVKPDEDVEI FLNRGLSTLK 

       370        380        390        400        410        420 
NESDVLIMGA FNEWRYRSFT TRLTETHLNG DWWSCKIHVP KEAYRADFVF FNGQDVYDNN 

       430        440        450        460        470        480 
DGNDFSITVK GGMQIIDFEN FLLEEKWREQ EKLAKEQAER ERLAEEQRRI EAEKAEIEAD 

       490        500        510        520        530        540 
RAQAKEEAAK KKKVLRELMV KATKTRDITW YIEPSEFKCE DKVRLYYNKS SGPLSHAKDL 

       550        560        570        580        590        600 
WIHGGYNNWK DGLSIVKKLV KSERIDGDWW YTEVVIPDQA LFLDWVFADG PPKHAIAYDN 

       610        620        630        640        650        660 
NHRQDFHAIV PNHIPEELYW VEEEHQIFKT LQEERRLREA AMRAKVEKTA LLKTETKERT 

       670        680        690        700        710        720 
MKSFLLSQKH VVYTEPLDIQ AGSSVTVYYN PANTVLNGKP EIWFRCSFNR WTHRLGPLPP 

       730        740        750        760        770        780 
QKMSPAENGT HVRATVKVPL DAYMMDFVFS EREDGGIFDN KSGMDYHIPV FGGVAKEPPM 

       790        800        810        820        830        840 
HIVHIAVEMA PIAKVGGLGD VVTSLSRAVQ DLNHNVDIIL PKYDCLKMNN VKDFRFHKNY 

       850        860        870        880        890        900 
FWGGTEIKVW FGKVEGLSVY FLEPQNGLFS KGCVYGCSND GERFGFFCHA ALEFLLQGGF 

       910        920        930        940        950        960 
SPDIIHCHDW SSAPVAWLFK EQYTHYGLSK SRIVFTIHNL EFGADLIGRA MTNADKATTV 

       970        980        990       1000       1010       1020 
SPTYSQEVSG NPVIAPHLHK FHGIVNGIDP DIWDPLNDKF IPIPYTSENV VEGKTAAKEA 

      1030       1040       1050       1060       1070       1080 
LQRKLGLKQA DLPLVGIITR LTHQKGIHLI KHAIWRTLER NGQVVLLGSA PDPRVQNNFV 

      1090       1100       1110       1120       1130       1140 
NLANQLHSKY NDRARLCLTY DEPLSHLIYA GADFILVPSI FEPCGLTQLT AMRYGSIPVV 

      1150       1160       1170       1180       1190       1200 
RKTGGLYDTV FDVDHDKERA QQCGLEPNGF SFDGADAGGV DYALNRALSA WYDGRDWFNS 

      1210       1220       1230 
LCKQVMEQDW SWNRPALDYL ELYHAARKLE

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References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X95759 mRNA. Translation: CAA65065.1. X94400 mRNA. Translation: CAA64173.1.
PIR	T07663.
3D structure databases
ProteinModelPortal	Q43846.
ModBase	Search...
Protein family/group databases
CAZy	CBM53. Carbohydrate-Binding Module Family 53. GT5. Glycosyltransferase Family 5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-1884.
UniPathway	UPA00152.
Family and domain databases
InterPro	IPR005085. CBM_fam25. IPR001296. Glyco_trans_1. IPR011835. Glycogen/starch_synth. IPR013534. Starch_synth_cat_dom. [Graphical view]
Pfam	PF03423. CBM_25. 3 hits. PF08323. Glyco_transf_5. 1 hit. PF00534. Glycos_transf_1. 1 hit. [Graphical view]
SMART	SM01066. CBM_25. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SSY3_SOLTU

Accession

Primary (citable) accession number: Q43846
Secondary accession number(s): O04842

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents