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Q9LKJ3 (PHSH_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-glucan phosphorylase, H isozyme

EC=2.4.1.1
Alternative name(s):
Starch phosphorylase H
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length832 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionGlycosyltransferase
Transferase
   Technical termAllosteric enzyme
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 – 832832Alpha-glucan phosphorylase, H isozyme
PRO_0000188543

Amino acid modifications

Modified residue6781N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9LKJ3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: BEF45CA8EDCBB466

FASTA83293,612
        10         20         30         40         50         60 
MSAADKVKPA ASPASEDPSA IAGNISYHAQ YSPHFSPLAF GPEQAFYATA ESVRDHLLQR 

        70         80         90        100        110        120 
WNDTYLHFHK TDPKQTYYLS MEYLQGRALT NAVGNLAITG AYADALKKFG YELEAIAGQE 

       130        140        150        160        170        180 
RDAALGNGGL GRLASCFLDS MATLNLPSWG YGLRYRYGLF KQRIAKEGQE EIAEDWLDKF 

       190        200        210        220        230        240 
SPWEIVRHDV VYPIRFFGHV EISPDGKRKW AGGEVLNALA YDVPIPGYKT KNAISLRLWD 

       250        260        270        280        290        300 
ATATAEDFNL FQFNDGQYES AAQLHSRAQQ ICAVLYPGDA TEEGKLLRLK QQYFLCSASL 

       310        320        330        340        350        360 
QDIIFRFKER KADRVSGKWS EFPSKVAVQM NDTHPTLAIP ELMRLLMDVE GLGWDEAWAV 

       370        380        390        400        410        420 
TNKTVAYTNH TVLPEALEKW SQAVMKKLLP RHMEIIEEID KRFREMVIST RKDMEGKIES 

       430        440        450        460        470        480 
MRVLDNNPEK PVVRMANLCV VAGHTVNGVA ELHSNILKQE LFADYVSIWP NKFQNKTNGI 

       490        500        510        520        530        540 
TPRRWLRFCN PELSEIVTKW LKTDQWTSNL DLLTGLRKFA DDEKLHAEWA AAKLASKKRL 

       550        560        570        580        590        600 
AKHVLDVTGV TIDPDSLFDI QIKRIHEYKR QLMNILGAVY RYKKLKEMSA ADRQKVTPRT 

       610        620        630        640        650        660 
VMVGGKAFAT YTNAKRIVKL VNDVGAVVNN DADVNKYLKV VFIPNYNVSV AEVLIPGSEL 

       670        680        690        700        710        720 
SQHISTAGME ASGTSNMKFS LNGCVIIGTL DGANVEIREE VGQDNFFLFG AKADQVAGLR 

       730        740        750        760        770        780 
KDRENGLFKP DPRFEEAKQF IRSGAFGTYD YTPLLDSLEG NTGFGRGDYF LVGYDFPSYI 

       790        800        810        820        830 
DAQARVDEAY KDKKKWVKMS ILNTAGSGKF SSDRTIDQYA KEIWGISACP VP 

« Hide

References

[1]"Full length clone of a cytosolic wheat leaf starch phosphorylase."
Schupp N.T., Ziegler P., Huebsch S.D.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Star.
Tissue: Leaf.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF275551 mRNA. Translation: AAF82787.1.
UniGeneTa.1197.

3D structure databases

ProteinModelPortalQ9LKJ3.
ModBaseSearch...

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ9LKJ3.

Enzyme and pathway databases

BRENDA2.4.1.1. 6500.

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_WHEAT
AccessionPrimary (citable) accession number: Q9LKJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: October 1, 2000
Last modified: May 31, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families