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P0AC86 (PHSG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen phosphorylase
EC=2.4.1.1
Gene names
Name:glgP
Synonyms:glgY
Ordered Locus Names:b3428, JW3391
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence caution

The sequence CAA34807.1 differs from that shown. Reason: Frameshift at position 9.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glycogen metabolism
   LigandPyridoxal phosphate
   Molecular functionGlycosyltransferase
Transferase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycogen catabolic process

Inferred from direct assay. Source: EcoliWiki

   Cellular componentcytoplasm

Inferred from direct assay Ref.2. Source: EcoliWiki

   Molecular functionglycogen phosphorylase activity

Inferred from direct assay Ref.2. Source: EcoliWiki

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 815815Glycogen phosphorylase
PRO_0000188553

Amino acid modifications

Modified residue6621N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict13 – 142SV → RL Ref.1
Sequence conflict601S → P in AAA23875. Ref.5
Sequence conflict94 – 952IY → TH in AAA23875. Ref.5
Sequence conflict1421L → W in AAA23875. Ref.5
Sequence conflict1751Y → S in CAA34807. Ref.1
Sequence conflict182 – 1876Missing in AAA23874. Ref.2
Sequence conflict1911R → V in CAA34807. Ref.1
Sequence conflict2481N → D in AAA23875. Ref.5
Sequence conflict280 – 2812EL → DV in AAA23874. Ref.2
Sequence conflict280 – 2812EL → DV in AAA58226. Ref.2
Sequence conflict2801E → G in AAA23875. Ref.5
Sequence conflict3241P → S in AAA23875. Ref.5
Sequence conflict3771I → S in AAA23875. Ref.5
Sequence conflict4501F → L in AAA23874. Ref.2
Sequence conflict487 – 4882EH → GT in CAA34807. Ref.1
Sequence conflict520 – 5212KL → NV in CAA34807. Ref.1
Sequence conflict7291S → T in AAA23874. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0AC86 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: B8046B91D8D7B468

FASTA81593,173
        10         20         30         40         50         60 
MNAPFTYSSP TLSVEALKHS IAYKLMFTIG KDPVVANKHE WLNATLFAVR DRLVERWLRS 

        70         80         90        100        110        120 
NRAQLSQETR QVYYLSMEFL IGRTLSNAML SLGIYEDVQG ALEAMGLNLE ELIDEENDPG 

       130        140        150        160        170        180 
LGNGGLGRLA ACFLDSLATL GLPGRGYGIR YDYGMFKQNI VNGSQKESPD YWLEYGNPWE 

       190        200        210        220        230        240 
FKRHNTRYKV RFGGRIQQEG KKTRWIETEE ILGVAYDQII PGYDTDATNT LRLWSAQASS 

       250        260        270        280        290        300 
EINLGKFNQG DYFAAVEDKN HSENVSRVLY PDDSTYSGRE LRLRQEYFLV SSTIQDILSR 

       310        320        330        340        350        360 
HYQLHKTYDN LADKIAIHLN DTHPVLSIPE MMRLLIDEHQ FSWDDAFEVC CQVFSYTNHT 

       370        380        390        400        410        420 
LMSEALETWP VDMLGKILPR HLQIIFEIND YFLKTLQEQY PNDTDLLGRA SIIDESNGRR 

       430        440        450        460        470        480 
VRMAWLAVVV SHKVNGVSEL HSNLMVQSLF ADFAKIFPGR FTNVTNGVTP RRWLAVANPS 

       490        500        510        520        530        540 
LSAVLDEHLG RNWRTDLSLL NELQQHCDFP MVNHAVHQAK LENKKRLAEY IAQQLNVVVN 

       550        560        570        580        590        600 
PKALFDVQIK RIHEYKRQLM NVLHVITRYN RIKADPDAKW VPRVNIFGGK AASAYYMAKH 

       610        620        630        640        650        660 
IIHLINDVAK VINNDPQIGD KLKVVFIPNY SVSLAQLIIP AADLSEQISL AGTEASGTSN 

       670        680        690        700        710        720 
MKFALNGALT IGTLDGANVE MLDHVGADNI FIFGNTAEEV EELRRQGYKP REYYEKDEEL 

       730        740        750        760        770        780 
HQVLTQIGSG VFSPEDPGRY RDLVDSLINF GDHYQVLADY RSYVDCQDKV DELYELQEEW 

       790        800        810 
TAKAMLNIAN MGYFSSDRTI KEYADHIWHI DPVRL

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of the glycogen phosphorylase gene from Escherichia coli."
Choi Y.-L., Kawamukai M., Utsumi R., Sakai H., Komano T.
FEBS Lett. 243:193-198(1989) [PubMed: 2645169] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Alpha-glucan phosphorylase from Escherichia coli. Cloning of the gene, and purification and characterization of the protein."
Yu F., Jen Y., Takeuchi E., Inouye M., Nakayama H., Tagaya M., Fukui T.
J. Biol. Chem. 263:13706-13711(1988) [PubMed: 3047129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Analysis of the Escherichia coli glycogen gene cluster suggests that catabolic enzymes are encoded among the biosynthetic genes."
Romeo T., Kumar A., Preiss J.
Gene 70:363-376(1988) [PubMed: 2975249] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-383.
Strain: K12.
[6]"Nucleotide sequence of the glycerol-3-phosphate dehydrogenase gene of Escherichia coli and regulation by the cAMP-CRP complex."
Choi Y.-L., Kawase S., Kawamukai M., Utsumi R., Sakai H., Komano T.
Agric. Biol. Chem. 53:1135-1143(1989)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 657-815.
[7]"Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose:alpha-1,4-glucan, 4-glucosyltransferase as deduced from the nucleotide sequence of the glgA gene."
Kumar A., Larsen C.E., Preiss J.
J. Biol. Chem. 261:16256-16259(1986) [PubMed: 3097003] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X16931 Genomic DNA. Translation: CAA34807.1. Frameshift.
J03966 Genomic DNA. Translation: AAA23874.1.
U18997 Genomic DNA. Translation: AAA58226.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC76453.1.
AP009048 Genomic DNA. Translation: BAE77864.1.
M22368 Genomic DNA. Translation: AAA23875.1.
D00425 Genomic DNA. Translation: BAA00329.1.
J02616 Genomic DNA. Translation: AAA23871.1.
PIRPHECGG. G65138.
RefSeqNP_417886.1. NC_000913.2.

3D structure databases

ProteinModelPortalP0AC86.
SMRP0AC86. Positions 12-815.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47899N.
IntActP0AC86. 1 interaction.
MINTMINT-1307808.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003797; EBESCP00000003797; EBESCG00000003104.
EBESCT00000003798; EBESCP00000003798; EBESCG00000003104.
EBESCT00000003799; EBESCP00000003799; EBESCG00000003104.
EBESCT00000015041; EBESCP00000014332; EBESCG00000014101.
GeneID947931.
GenomeReviewsGene locus JW3391 in contig AP009048_GR.
Gene locus b3428 in contig U00096_GR.
KEGGecj:JW3391.
eco:b3428.
PATRIC32122296. VBIEscCol129921_3525.

Organism-specific databases

EchoBASEEB0375.
EcoGeneEG10380. glgP.

Phylogenomic databases

eggNOGCOG0058.
GeneTreeEBGT00050000009895.
HOGENOMHBG444050.
OMAAAFMDSL.
PhylomeDBP0AC86.
ProtClustDBPRK14986.

Enzyme and pathway databases

BioCycEcoCyc:GLYCOPHOSPHORYL-MONOMER.
MetaCyc:GLYCOPHOSPHORYL-MONOMER.

Gene expression databases

GenevestigatorP0AC86.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
KOK00688.
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 namePHSG_ECOLI
AccessionPrimary (citable) accession number: P0AC86
Secondary accession number(s): P13031, Q2M792
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

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