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P00489 (PYGM_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

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

Names and origin

Protein namesRecommended name:
Glycogen phosphorylase, muscle form

EC=2.4.1.1
Alternative name(s):
Myophosphorylase
Gene names
Name:PYGM
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Enzyme regulation

Activity of phosphorylase is controlled both by allosteric means (through the noncovalent binding of metabolites) and by covalent modification. Thus AMP allosterically activates, whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit, phosphorylase B.

Subunit structure

Homodimer. Dimers associate into a tetramer to form the enzymatically active phosphorylase A.

Post-translational modification

Phosphorylation of Ser-15 converts phosphorylase B (unphosphorylated) to phosphorylase A.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 843842Glycogen phosphorylase, muscle form
PRO_0000188532

Sites

Binding site761AMP
Site1091Involved in the association of subunits
Site1431Involved in the association of subunits
Site1561Can be labeled by an AMP analog; may be involved in allosteric regulation

Amino acid modifications

Modified residue21N-acetylserine Ref.1
Modified residue151Phosphoserine; by PHK; in form phosphorylase A Ref.2
Modified residue4731Phosphotyrosine By similarity
Modified residue6811N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict31 – 333NFN → DFD AA sequence Ref.2
Sequence conflict431D → N AA sequence Ref.2
Sequence conflict56 – 583LAH → HAL AA sequence Ref.2
Sequence conflict891E → Q AA sequence Ref.2
Sequence conflict1131T → D AA sequence Ref.2
Sequence conflict3091Missing AA sequence Ref.2
Sequence conflict578 – 5792LL → FF in CAA26833. Ref.6
Sequence conflict6101A → P in BAA00027. Ref.1
Sequence conflict6101A → P in CAA27816. Ref.1
Sequence conflict7131G → C in CAA26833. Ref.6

Secondary structure

................................................................................................................................................................ 843
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00489 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9884F06FDD3AE9D3

FASTA84397,289
        10         20         30         40         50         60 
MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV 

        70         80         90        100        110        120 
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM 

       130        140        150        160        170        180 
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA 

       190        200        210        220        230        240 
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN 

       250        260        270        280        290        300 
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 

       310        320        330        340        350        360 
VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL MRVLVDLERL 

       370        380        390        400        410        420 
DWDKAWEVTV KTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP 

       430        440        450        460        470        480 
GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS HAVNGVARIH SEILKKTIFK DFYELEPHKF 

       490        500        510        520        530        540 
QNKTNGITPR RWLVLCNPGL AEIIAERIGE EYISDLDQLR KLLSYVDDEA FIRDVAKVKQ 

       550        560        570        580        590        600 
ENKLKFAAYL EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFVV 

       610        620        630        640        650        660 
PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA 

       670        680        690        700        710        720 
ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD 

       730        740        750        760        770        780 
RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADYEE 

       790        800        810        820        830        840 
YVKCQERVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE 


KIP 

« Hide

References

[1]"Complete cDNA sequence for rabbit muscle glycogen phosphorylase."
Nakano K., Hwang P.K., Fletterick R.J.
FEBS Lett. 204:283-287(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence of the amino-terminal 349 residues of rabbit muscle glycogen phosphorylase including the sites of covalent and allosteric control."
Koide A., Titani K., Ericsson L.H., Kumar S., Neurath H., Walsh K.A.
Biochemistry 17:5657-5672(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-351.
[3]"Amino acid sequence of two cyanogen bromide fragments of glycogen phosphorylase."
Hermann J., Titani K., Ericsson L.H., Wade R.D., Neurath H., Walsh K.A.
Biochemistry 17:5672-5679(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 352-429 AND 443-605.
[4]"Sequence of the carboxyl-terminal 492 residues of rabbit muscle glycogen phosphorylase including the pyridoxal 5'-phosphate binding site."
Titani K., Koide A., Ericsson L.H., Kumar S., Hermann J., Wade R.D., Walsh K.A., Neurath H., Fischer E.H.
Biochemistry 17:5680-5693(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 352-843.
[5]"Inactivation of phosphorylase b by potassium ferrate. Identification of a tyrosine residue involved in the binding of adenosine 5'-monophosphate."
Lee Y.M., Benisek W.F.
J. Biol. Chem. 253:5460-5463(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 71-81.
[6]"Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs."
Hwang P.K., See Y.P., Vincentini A.M., Powers M.A., Fletterick R.J., Crerar M.M.
Eur. J. Biochem. 152:267-274(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 575-843.
[7]"Crystallographic analysis of phosphorylase alpha at 2.5-A resolution, a comment on the chemical sequence."
Sprang S.R., Fletterick R.J.
Biochemistry 17:5693-5694(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A.
[8]"Domain separation in the activation of glycogen phosphorylase a."
Goldsmith E.J., Sprang S.R., Hamlin R., Xuong N.-H., Fletterick R.J.
Science 245:528-532(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF PHOSPHORYLASE A.
[9]"Structure of the nucleotide activation switch in glycogen phosphorylase a."
Sprang S.R., Goldsmith E.J., Fletterick R.J.
Science 237:1012-1019(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF PHOSPHORYLASE A WITH AMP.
[10]"Assignment of the amino acid sequence to the crystal structure of glycogen phosphorylase b."
Jenkins J.A., Johnson L.N., Wilson K.S.
Biochemistry 17:5694-5695(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF PHOSPHORYLASE B.
[11]"The binding of 2-deoxy-D-glucose 6-phosphate to glycogen phosphorylase b: kinetic and crystallographic studies."
Oikonomakos N.G., Zographos S.E., Johnson L.N., Papageorgiou A.C., Acharya K.R.
J. Mol. Biol. 254:900-917(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF PHOSPHORYLASE B.
[12]"Activator anion binding site in pyridoxal phosphorylase b: the binding of phosphite, phosphate, and fluorophosphate in the crystal."
Oikonomakos N.G., Zographos S.E., Tsitsanou K.E., Johnson L.N., Acharya K.R.
Protein Sci. 5:2416-2428(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF PHOSPHORYLASE B.
[13]"The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8-A resolution and 100 K: the role of the water structure and its contribution to binding."
Gregoriou M., Noble M.E.M., Watson K.A., Garman E.F., Krulle T.M., de la Fuente C., Fleet G.W., Oikonomakos N.G., Johnson L.N.
Protein Sci. 7:915-927(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF PHOSPHORYLASE B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00040 mRNA. Translation: BAA00027.1.
X04265 mRNA. Translation: CAA27816.1.
X03030 mRNA. Translation: CAA26833.1.
PIRPHRBG. A24302.
RefSeqNP_001075653.1. NM_001082184.1.
UniGeneOcu.2087.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8IX-ray1.78A2-843[»]
1ABBX-ray2.80A/B/C/D11-838[»]
1AXRX-ray2.30A2-843[»]
1B4DX-ray2.00A2-843[»]
1BX3X-ray2.30A2-843[»]
1C50X-ray2.30A14-843[»]
1C8KX-ray1.76A2-843[»]
1C8LX-ray2.30A2-843[»]
1E1YX-ray2.23A2-843[»]
1FS4X-ray2.38A2-843[»]
1FTQX-ray2.35A2-843[»]
1FTWX-ray2.36A2-843[»]
1FTYX-ray2.38A2-843[»]
1FU4X-ray2.36A2-843[»]
1FU7X-ray2.36A2-843[»]
1FU8X-ray2.35A2-843[»]
1GFZX-ray2.30A2-843[»]
1GG8X-ray2.31A2-843[»]
1GGNX-ray2.36A2-843[»]
1GPAX-ray2.90A/B/C/D2-843[»]
1GPBX-ray1.90A2-843[»]
1GPYX-ray2.40A2-843[»]
1H5UX-ray1.76A2-843[»]
1HLFX-ray2.26A2-843[»]
1K06X-ray1.80A2-843[»]
1K08X-ray2.26A2-843[»]
1KTIX-ray1.97A2-843[»]
1LWNX-ray2.00A2-843[»]
1LWOX-ray2.00A2-843[»]
1NOIX-ray2.50A/B/C/D2-843[»]
1NOJX-ray2.40A2-843[»]
1NOKX-ray2.40A2-843[»]
1P29X-ray2.20A2-843[»]
1P2BX-ray2.20A2-843[»]
1P2DX-ray1.94A2-843[»]
1P2GX-ray2.30A2-843[»]
1P4GX-ray2.10A2-843[»]
1P4HX-ray2.06A2-843[»]
1P4JX-ray2.00A2-843[»]
1PYGX-ray2.87A/B/C/D2-843[»]
1UZUX-ray2.30A2-843[»]
1WUTX-ray2.26A2-843[»]
1WUYX-ray2.26A2-843[»]
1WV0X-ray2.26A2-843[»]
1WV1X-ray2.26A2-843[»]
1WW2X-ray1.90A2-843[»]
1WW3X-ray1.80A2-843[»]
1XC7X-ray1.83A2-843[»]
1XKXX-ray1.93A2-843[»]
1XL0X-ray1.92A2-843[»]
1XL1X-ray2.10A2-843[»]
1Z62X-ray1.90A2-843[»]
1Z6PX-ray2.40A2-843[»]
1Z6QX-ray2.03A2-843[»]
2AMVX-ray2.30A2-843[»]
2F3PX-ray1.94A2-843[»]
2F3QX-ray1.96A2-843[»]
2F3SX-ray1.96A2-843[»]
2F3UX-ray1.93A2-843[»]
2FETX-ray2.03A2-843[»]
2FF5X-ray2.03A2-843[»]
2FFRX-ray2.03A13-837[»]
2G9QX-ray2.50A2-843[»]
2G9RX-ray2.07A2-843[»]
2G9UX-ray2.15A2-843[»]
2G9VX-ray2.15A2-843[»]
2GJ4X-ray1.60A13-836[»]
2GM9X-ray2.30A13-837[»]
2GPAX-ray2.00A2-839[»]
2GPBX-ray2.30A2-843[»]
2GPNX-ray1.99A2-843[»]
2IEGX-ray1.90A/B2-843[»]
2IEIX-ray1.91A/B2-843[»]
2OFFX-ray2.20A2-843[»]
2PRIX-ray2.30A2-843[»]
2PRJX-ray2.30A2-843[»]
2PYDX-ray1.93A1-843[»]
2PYIX-ray1.88A1-843[»]
2QLMX-ray2.10A2-843[»]
2QLNX-ray2.15A2-843[»]
2QN1X-ray2.40A2-843[»]
2QN2X-ray2.70A2-843[»]
2QN3X-ray1.96A2-843[»]
2QN7X-ray1.83A2-843[»]
2QN8X-ray1.90A2-843[»]
2QN9X-ray2.00A2-843[»]
2QNBX-ray1.80A2-843[»]
2QRGX-ray1.85A2-843[»]
2QRHX-ray1.83A2-843[»]
2QRMX-ray1.90A2-843[»]
2QRPX-ray1.86A2-843[»]
2QRQX-ray1.80A2-843[»]
2SKCX-ray2.40A2-843[»]
2SKDX-ray2.40A2-843[»]
2SKEX-ray2.46A2-843[»]
3AMVX-ray2.10A2-843[»]
3BCRX-ray2.14A2-843[»]
3BCSX-ray2.00A2-843[»]
3BCUX-ray2.03A2-843[»]
3BD6X-ray2.00A2-843[»]
3BD7X-ray1.90A2-843[»]
3BD8X-ray2.10A2-843[»]
3BDAX-ray2.00A2-843[»]
3CUTX-ray2.30A2-843[»]
3CUUX-ray2.30A2-843[»]
3CUVX-ray1.93A2-843[»]
3CUWX-ray2.00A2-843[»]
3E3LX-ray2.59A/B/C/D2-843[»]
3E3NX-ray2.70A/B/C/D/E/F/G/H2-843[»]
3E3OX-ray2.60A/B/C/D2-843[»]
3EBOX-ray1.90A2-843[»]
3EBPX-ray2.00A2-843[»]
3G2HX-ray2.03A2-843[»]
3G2IX-ray2.00A2-843[»]
3G2JX-ray2.14A2-843[»]
3G2KX-ray2.00A2-843[»]
3G2LX-ray2.30A2-843[»]
3G2NX-ray2.10A2-843[»]
3GPBX-ray2.30A2-843[»]
3L79X-ray1.86A1-843[»]
3L7AX-ray1.90A1-843[»]
3L7BX-ray2.00A1-843[»]
3L7CX-ray1.93A1-843[»]
3L7DX-ray2.00A1-843[»]
3MQFX-ray1.95A2-843[»]
3MRTX-ray1.98A2-843[»]
3MRVX-ray1.94A2-843[»]
3MRXX-ray1.95A2-843[»]
3MS2X-ray2.10A2-843[»]
3MS4X-ray2.07A2-843[»]
3MS7X-ray1.95A2-843[»]
3MSCX-ray1.95A2-843[»]
3MT7X-ray2.00A2-843[»]
3MT8X-ray2.00A2-843[»]
3MT9X-ray2.05A2-843[»]
3MTAX-ray2.23A2-843[»]
3MTBX-ray1.95A2-843[»]
3MTDX-ray2.10A2-843[»]
3NC4X-ray2.07A3-843[»]
3NP7X-ray2.05A2-843[»]
3NP9X-ray2.00A2-843[»]
3NPAX-ray1.97A2-843[»]
3S0JX-ray2.00A2-843[»]
3SYMX-ray2.40A2-843[»]
3SYRX-ray2.40A2-843[»]
3T3DX-ray2.50A2-843[»]
3T3EX-ray2.15A2-843[»]
3T3GX-ray2.40A2-843[»]
3T3HX-ray2.60A2-843[»]
3T3IX-ray2.65A2-843[»]
3ZCPX-ray1.83A1-843[»]
3ZCQX-ray2.15A1-843[»]
3ZCRX-ray2.07A1-843[»]
3ZCSX-ray2.03A1-843[»]
3ZCTX-ray2.00A1-843[»]
3ZCUX-ray2.05A1-843[»]
3ZCVX-ray1.83A1-843[»]
4EJ2X-ray2.65A13-837[»]
4EKEX-ray2.60A13-837[»]
4EKYX-ray2.45A13-837[»]
4EL0X-ray2.40A13-837[»]
4EL5X-ray2.00A13-837[»]
4GPBX-ray2.30A2-843[»]
4MRAX-ray2.34A13-837[»]
5GPBX-ray2.30A2-843[»]
6GPBX-ray2.86A2-843[»]
7GPBX-ray2.90A/B/C/D2-843[»]
8GPBX-ray2.20A2-843[»]
9GPBX-ray2.90A/B/C/D2-843[»]
ProteinModelPortalP00489.
SMRP00489. Positions 15-843.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-38240N.
IntActP00489. 2 interactions.
MINTMINT-6368963.

Chemistry

BindingDBP00489.
ChEMBLCHEMBL4696.
DrugBankDB00131. Adenosine monophosphate.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Proteomic databases

PRIDEP00489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008972.

Organism-specific databases

CTD5837.

Phylogenomic databases

eggNOGCOG0058.
HOGENOMHOG000278444.
HOVERGENHBG006848.

Enzyme and pathway databases

BRENDA2.4.1.1. 1749.
SABIO-RKP00489.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. PTHR11468. 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...

Other

EvolutionaryTraceP00489.

Entry information

Entry namePYGM_RABIT
AccessionPrimary (citable) accession number: P00489
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references