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Reviewed, UniProtKB/Swiss-Prot P32811 (PHSH_SOLTU)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Alpha-glucan phosphorylase, H isozyme
    EC=2.4.1.1
Alternative name(s):
    Starch phosphorylase H
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Catalytic activity

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

Cofactor

Pyridoxal phosphate.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionGlycosyltransferase
Transferase
   Technical termAllosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionphosphorylase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 838838Alpha-glucan phosphorylase, H isozyme
PRO_0000188542

Amino acid modifications

Modified residue6841N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P32811-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 1F3A55BE0F0167B4

FASTA83895,112
        10         20         30         40         50         60 
MEGGAKSNDV SAAPIAQPLS EDPTDIASNI KYHAQYTPHF SPFKFEPLQA YYAATADSVR 

        70         80         90        100        110        120 
DRLIKQWNDT YLHYDKVNPK QTYYLSMEYL QGRALTNAVG NLDIHNAYAD ALNKLGQQLE 

       130        140        150        160        170        180 
EVVEQEKDAA LGNGGLGRLA SCFLDSMATL NLPAWGYGLR YRYGLFKQLI TKAGQEEVPE 

       190        200        210        220        230        240 
DWLEKFSPWE IVRHDVVFPI RFFGHVEVLP SGSRKWVGGE VLQALAYDVP IPGYRTKNTN 

       250        260        270        280        290        300 
SLRLWEAKAS SEDFNLFLFN DGQYDAAAQL HSRAQQICAV LYPGDATENG KLLRLKQQFF 

       310        320        330        340        350        360 
LCSASLQDII ARFKEREDGK GSHQWSEFPK KVAIQLNDTH PTLTIPELMR LLMDDEGLGW 

       370        380        390        400        410        420 
DESWNITTRT IAYTNHTVLP EALEKWSQAV MWKLLPRHME IIEEIDKRFV ATIMSERPDL 

       430        440        450        460        470        480 
ENKMPSMRIL DHNATKPVVH MANLCVVSSH TVNGVAQLHS DILKAELFAD YVSVWPTKFQ 

       490        500        510        520        530        540 
NKTNGITPRR WIRFCSPELS HIITKWLKTD QWVTNLELLA NLREFADNSE LHAEWESAKM 

       550        560        570        580        590        600 
ANKQRLAQYI LHVTGVSIDP NSLFDIQVKR IHEYKRQLLN ILGVIYRYKK LKGMSPEERK 

       610        620        630        640        650        660 
NTTPRTVMIG GKAFATYTNA KRIVKLVTDV GDVVNSDPDV NDYLKVVFVP NYNVSVAEML 

       670        680        690        700        710        720 
IPGSELSQHI STAGMEASGT SNMKFALNGC LIIGTLDGAN VEIREEIGED NFFLFGATAD 

       730        740        750        760        770        780 
EVPQLRKDRE NGLFKPDPRF EEAKQFIRSG AFGTYDYNPL LESLEGNSGY GRGDYFLVGH 

       790        800        810        820        830 
DFPSYMDAQA RVDEAYKDRK RWIKMSILST SGSGKFSSDR TISQYAKEIW NIAECRVP 

« Hide

References

[1]"Potato tuber type H phosphorylase isozyme. Molecular cloning, nucleotide sequence, and expression of a full-length cDNA in Escherichia coli."
Mori H., Tanizawa K., Fukui T.
J. Biol. Chem. 266:18446-18453(1991) [PubMed: 1917968] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

M69038 mRNA. Translation: AAA33809.1.
PIRA40995.

3D structure databases

HSSPHSSP built from PDB template 1YGP based on UniProtKB P06738.
ModBaseSearch...

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Enzyme and pathway databases

BRENDA2.4.1.1. 296.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. Glyco_trans_35. 1 hit.
PfamPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsTIGR02093. P_ylase. 1 hit.
PROSITEPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHSH_SOLTU
AccessionPrimary (citable) accession number: P32811
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents