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P00489

- PYGM_RABIT

UniProt

P00489 - PYGM_RABIT

Protein

Glycogen phosphorylase, muscle form

Gene

PYGM

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Cofactori

    Pyridoxal phosphate.

    Enzyme regulationi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei76 – 761AMP
    Sitei109 – 1091Involved in the association of subunits
    Sitei143 – 1431Involved in the association of subunits
    Sitei156 – 1561Can be labeled by an AMP analog; may be involved in allosteric regulation

    GO - Molecular functioni

    1. glycogen phosphorylase activity Source: Ensembl
    2. nucleotide binding Source: UniProtKB-KW
    3. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. glycogen catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Keywords - Ligandi

    Nucleotide-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi2.4.1.1. 1749.
    SABIO-RKP00489.

    Protein family/group databases

    CAZyiGT35. Glycosyltransferase Family 35.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycogen phosphorylase, muscle form (EC:2.4.1.1)
    Alternative name(s):
    Myophosphorylase
    Gene namesi
    Name:PYGM
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 843842Glycogen phosphorylase, muscle formPRO_0000188532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei15 – 151Phosphoserine; by PHK; in form phosphorylase A
    Modified residuei473 – 4731PhosphotyrosineBy similarity
    Modified residuei681 – 6811N6-(pyridoxal phosphate)lysine

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP00489.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-38240N.
    IntActiP00489. 2 interactions.
    MINTiMINT-6368963.

    Structurei

    Secondary structure

    1
    843
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 135
    Helixi15 – 173
    Helixi22 – 3817
    Turni44 – 463
    Helixi49 – 6214
    Helixi65 – 7814
    Beta strandi82 – 865
    Beta strandi90 – 934
    Helixi96 – 1027
    Helixi106 – 11510
    Helixi120 – 1245
    Beta strandi130 – 1323
    Helixi136 – 15015
    Beta strandi155 – 1606
    Beta strandi168 – 1725
    Beta strandi175 – 1795
    Turni183 – 1864
    Helixi195 – 1973
    Beta strandi199 – 2046
    Beta strandi206 – 2094
    Beta strandi211 – 2188
    Beta strandi220 – 23213
    Beta strandi234 – 2374
    Beta strandi239 – 24810
    Helixi253 – 2564
    Beta strandi259 – 2613
    Helixi263 – 2686
    Helixi270 – 2745
    Helixi275 – 2773
    Beta strandi284 – 2863
    Helixi291 – 31323
    Turni315 – 3195
    Beta strandi322 – 3254
    Helixi327 – 3293
    Helixi330 – 3334
    Beta strandi334 – 3418
    Turni342 – 3454
    Helixi346 – 35611
    Helixi362 – 37211
    Beta strandi373 – 3764
    Helixi382 – 3843
    Beta strandi387 – 3893
    Helixi390 – 3967
    Helixi398 – 41821
    Beta strandi419 – 4213
    Helixi423 – 4297
    Beta strandi431 – 4333
    Beta strandi435 – 4373
    Beta strandi439 – 4413
    Helixi442 – 4487
    Beta strandi453 – 4575
    Helixi458 – 4669
    Turni467 – 4693
    Helixi470 – 4756
    Helixi477 – 4793
    Beta strandi480 – 4823
    Helixi490 – 4956
    Helixi498 – 50811
    Helixi511 – 5144
    Helixi516 – 52510
    Helixi529 – 55426
    Beta strandi562 – 5698
    Turni573 – 5764
    Helixi577 – 59317
    Beta strandi602 – 6076
    Helixi615 – 63117
    Turni635 – 6373
    Helixi638 – 6403
    Beta strandi641 – 6466
    Helixi651 – 6577
    Helixi658 – 6603
    Beta strandi662 – 6665
    Turni670 – 6723
    Beta strandi673 – 6753
    Helixi678 – 6847
    Beta strandi688 – 6914
    Helixi697 – 7048
    Helixi706 – 7083
    Beta strandi709 – 7113
    Helixi716 – 72510
    Helixi729 – 7357
    Helixi737 – 74812
    Turni749 – 7513
    Beta strandi753 – 7553
    Turni756 – 7594
    Helixi760 – 7689
    Helixi775 – 7773
    Helixi778 – 79215
    Helixi795 – 80612
    Helixi810 – 8123
    Helixi814 – 82411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP00489.
    SMRiP00489. Positions 15-843.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00489.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycogen phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0058.
    HOGENOMiHOG000278444.
    HOVERGENiHBG006848.

    Family and domain databases

    InterProiIPR011833. Glycg_phsphrylas.
    IPR000811. Glyco_trans_35.
    [Graphical view]
    PANTHERiPTHR11468. PTHR11468. 1 hit.
    PfamiPF00343. Phosphorylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
    TIGRFAMsiTIGR02093. P_ylase. 1 hit.
    PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00489-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRPLSDQEK RKQISVRGLA GVENVTELKK NFNRHLHFTL VKDRNVATPR    50
    DYYFALAHTV RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM 100
    VNLALENACD EATYQLGLDM EELEEIEEDA GLGNGGLGRL AACFLDSMAT 150
    LGLAAYGYGI RYEFGIFNQK ICGGWQMEEA DDWLRYGNPW EKARPEFTLP 200
    VHFYGRVEHT SQGAKWVDTQ VVLAMPYDTP VPGYRNNVVN TMRLWSAKAP 250
    NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV 300
    VAATLQDIIR RFKSSKFGCR DPVRTNFDAF PDKVAIQLND THPSLAIPEL 350
    MRVLVDLERL DWDKAWEVTV KTCAYTNHTV LPEALERWPV HLLETLLPRH 400
    LQIIYEINQR FLNRVAAAFP GDVDRLRRMS LVEEGAVKRI NMAHLCIAGS 450
    HAVNGVARIH SEILKKTIFK DFYELEPHKF QNKTNGITPR RWLVLCNPGL 500
    AEIIAERIGE EYISDLDQLR KLLSYVDDEA FIRDVAKVKQ ENKLKFAAYL 550
    EREYKVHINP NSLFDVQVKR IHEYKRQLLN CLHVITLYNR IKKEPNKFVV 600
    PRTVMIGGKA APGYHMAKMI IKLITAIGDV VNHDPVVGDR LRVIFLENYR 650
    VSLAEKVIPA ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM 700
    AEEAGEENFF IFGMRVEDVD RLDQRGYNAQ EYYDRIPELR QIIEQLSSGF 750
    FSPKQPDLFK DIVNMLMHHD RFKVFADYEE YVKCQERVSA LYKNPREWTR 800
    MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SRQRLPAPDE KIP 843
    Length:843
    Mass (Da):97,289
    Last modified:January 23, 2007 - v3
    Checksum:i9884F06FDD3AE9D3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 333NFN → DFD AA sequence (PubMed:728424)Curated
    Sequence conflicti43 – 431D → N AA sequence (PubMed:728424)Curated
    Sequence conflicti56 – 583LAH → HAL AA sequence (PubMed:728424)Curated
    Sequence conflicti89 – 891E → Q AA sequence (PubMed:728424)Curated
    Sequence conflicti113 – 1131T → D AA sequence (PubMed:728424)Curated
    Sequence conflicti309 – 3091Missing AA sequence (PubMed:728424)Curated
    Sequence conflicti578 – 5792LL → FF in CAA26833. (PubMed:3840433)Curated
    Sequence conflicti610 – 6101A → P in BAA00027. (PubMed:3015680)Curated
    Sequence conflicti610 – 6101A → P in CAA27816. (PubMed:3015680)Curated
    Sequence conflicti713 – 7131G → C in CAA26833. (PubMed:3840433)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00040 mRNA. Translation: BAA00027.1.
    X04265 mRNA. Translation: CAA27816.1.
    X03030 mRNA. Translation: CAA26833.1.
    PIRiA24302. PHRBG.
    RefSeqiNP_001075653.1. NM_001082184.1.
    UniGeneiOcu.2087.

    Genome annotation databases

    GeneIDi100008972.

    Cross-referencesi

    Web resourcesi

    ProZyme technical fact sheet

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00040 mRNA. Translation: BAA00027.1 .
    X04265 mRNA. Translation: CAA27816.1 .
    X03030 mRNA. Translation: CAA26833.1 .
    PIRi A24302. PHRBG.
    RefSeqi NP_001075653.1. NM_001082184.1.
    UniGenei Ocu.2087.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A8I X-ray 1.78 A 2-843 [» ]
    1ABB X-ray 2.80 A/B/C/D 11-838 [» ]
    1AXR X-ray 2.30 A 2-843 [» ]
    1B4D X-ray 2.00 A 2-843 [» ]
    1BX3 X-ray 2.30 A 2-843 [» ]
    1C50 X-ray 2.30 A 14-843 [» ]
    1C8K X-ray 1.76 A 2-843 [» ]
    1C8L X-ray 2.30 A 2-843 [» ]
    1E1Y X-ray 2.23 A 2-843 [» ]
    1FS4 X-ray 2.38 A 2-843 [» ]
    1FTQ X-ray 2.35 A 2-843 [» ]
    1FTW X-ray 2.36 A 2-843 [» ]
    1FTY X-ray 2.38 A 2-843 [» ]
    1FU4 X-ray 2.36 A 2-843 [» ]
    1FU7 X-ray 2.36 A 2-843 [» ]
    1FU8 X-ray 2.35 A 2-843 [» ]
    1GFZ X-ray 2.30 A 2-843 [» ]
    1GG8 X-ray 2.31 A 2-843 [» ]
    1GGN X-ray 2.36 A 2-843 [» ]
    1GPA X-ray 2.90 A/B/C/D 2-843 [» ]
    1GPB X-ray 1.90 A 2-843 [» ]
    1GPY X-ray 2.40 A 2-843 [» ]
    1H5U X-ray 1.76 A 2-843 [» ]
    1HLF X-ray 2.26 A 2-843 [» ]
    1K06 X-ray 1.80 A 2-843 [» ]
    1K08 X-ray 2.26 A 2-843 [» ]
    1KTI X-ray 1.97 A 2-843 [» ]
    1LWN X-ray 2.00 A 2-843 [» ]
    1LWO X-ray 2.00 A 2-843 [» ]
    1NOI X-ray 2.50 A/B/C/D 2-843 [» ]
    1NOJ X-ray 2.40 A 2-843 [» ]
    1NOK X-ray 2.40 A 2-843 [» ]
    1P29 X-ray 2.20 A 2-843 [» ]
    1P2B X-ray 2.20 A 2-843 [» ]
    1P2D X-ray 1.94 A 2-843 [» ]
    1P2G X-ray 2.30 A 2-843 [» ]
    1P4G X-ray 2.10 A 2-843 [» ]
    1P4H X-ray 2.06 A 2-843 [» ]
    1P4J X-ray 2.00 A 2-843 [» ]
    1PYG X-ray 2.87 A/B/C/D 2-843 [» ]
    1UZU X-ray 2.30 A 2-843 [» ]
    1WUT X-ray 2.26 A 2-843 [» ]
    1WUY X-ray 2.26 A 2-843 [» ]
    1WV0 X-ray 2.26 A 2-843 [» ]
    1WV1 X-ray 2.26 A 2-843 [» ]
    1WW2 X-ray 1.90 A 2-843 [» ]
    1WW3 X-ray 1.80 A 2-843 [» ]
    1XC7 X-ray 1.83 A 2-843 [» ]
    1XKX X-ray 1.93 A 2-843 [» ]
    1XL0 X-ray 1.92 A 2-843 [» ]
    1XL1 X-ray 2.10 A 2-843 [» ]
    1Z62 X-ray 1.90 A 2-843 [» ]
    1Z6P X-ray 2.40 A 2-843 [» ]
    1Z6Q X-ray 2.03 A 2-843 [» ]
    2AMV X-ray 2.30 A 2-843 [» ]
    2F3P X-ray 1.94 A 2-843 [» ]
    2F3Q X-ray 1.96 A 2-843 [» ]
    2F3S X-ray 1.96 A 2-843 [» ]
    2F3U X-ray 1.93 A 2-843 [» ]
    2FET X-ray 2.03 A 2-843 [» ]
    2FF5 X-ray 2.03 A 2-843 [» ]
    2FFR X-ray 2.03 A 13-837 [» ]
    2G9Q X-ray 2.50 A 2-843 [» ]
    2G9R X-ray 2.07 A 2-843 [» ]
    2G9U X-ray 2.15 A 2-843 [» ]
    2G9V X-ray 2.15 A 2-843 [» ]
    2GJ4 X-ray 1.60 A 13-836 [» ]
    2GM9 X-ray 2.30 A 13-837 [» ]
    2GPA X-ray 2.00 A 2-839 [» ]
    2GPB X-ray 2.30 A 2-843 [» ]
    2GPN X-ray 1.99 A 2-843 [» ]
    2IEG X-ray 1.90 A/B 2-843 [» ]
    2IEI X-ray 1.91 A/B 2-843 [» ]
    2OFF X-ray 2.20 A 2-843 [» ]
    2PRI X-ray 2.30 A 2-843 [» ]
    2PRJ X-ray 2.30 A 2-843 [» ]
    2PYD X-ray 1.93 A 1-843 [» ]
    2PYI X-ray 1.88 A 1-843 [» ]
    2QLM X-ray 2.10 A 2-843 [» ]
    2QLN X-ray 2.15 A 2-843 [» ]
    2QN1 X-ray 2.40 A 2-843 [» ]
    2QN2 X-ray 2.70 A 2-843 [» ]
    2QN3 X-ray 1.96 A 2-843 [» ]
    2QN7 X-ray 1.83 A 2-843 [» ]
    2QN8 X-ray 1.90 A 2-843 [» ]
    2QN9 X-ray 2.00 A 2-843 [» ]
    2QNB X-ray 1.80 A 2-843 [» ]
    2QRG X-ray 1.85 A 2-843 [» ]
    2QRH X-ray 1.83 A 2-843 [» ]
    2QRM X-ray 1.90 A 2-843 [» ]
    2QRP X-ray 1.86 A 2-843 [» ]
    2QRQ X-ray 1.80 A 2-843 [» ]
    2SKC X-ray 2.40 A 2-843 [» ]
    2SKD X-ray 2.40 A 2-843 [» ]
    2SKE X-ray 2.46 A 2-843 [» ]
    3AMV X-ray 2.10 A 2-843 [» ]
    3BCR X-ray 2.14 A 2-843 [» ]
    3BCS X-ray 2.00 A 2-843 [» ]
    3BCU X-ray 2.03 A 2-843 [» ]
    3BD6 X-ray 2.00 A 2-843 [» ]
    3BD7 X-ray 1.90 A 2-843 [» ]
    3BD8 X-ray 2.10 A 2-843 [» ]
    3BDA X-ray 2.00 A 2-843 [» ]
    3CUT X-ray 2.30 A 2-843 [» ]
    3CUU X-ray 2.30 A 2-843 [» ]
    3CUV X-ray 1.93 A 2-843 [» ]
    3CUW X-ray 2.00 A 2-843 [» ]
    3E3L X-ray 2.59 A/B/C/D 2-843 [» ]
    3E3N X-ray 2.70 A/B/C/D/E/F/G/H 2-843 [» ]
    3E3O X-ray 2.60 A/B/C/D 2-843 [» ]
    3EBO X-ray 1.90 A 2-843 [» ]
    3EBP X-ray 2.00 A 2-843 [» ]
    3G2H X-ray 2.03 A 2-843 [» ]
    3G2I X-ray 2.00 A 2-843 [» ]
    3G2J X-ray 2.14 A 2-843 [» ]
    3G2K X-ray 2.00 A 2-843 [» ]
    3G2L X-ray 2.30 A 2-843 [» ]
    3G2N X-ray 2.10 A 2-843 [» ]
    3GPB X-ray 2.30 A 2-843 [» ]
    3L79 X-ray 1.86 A 1-843 [» ]
    3L7A X-ray 1.90 A 1-843 [» ]
    3L7B X-ray 2.00 A 1-843 [» ]
    3L7C X-ray 1.93 A 1-843 [» ]
    3L7D X-ray 2.00 A 1-843 [» ]
    3MQF X-ray 1.95 A 2-843 [» ]
    3MRT X-ray 1.98 A 2-843 [» ]
    3MRV X-ray 1.94 A 2-843 [» ]
    3MRX X-ray 1.95 A 2-843 [» ]
    3MS2 X-ray 2.10 A 2-843 [» ]
    3MS4 X-ray 2.07 A 2-843 [» ]
    3MS7 X-ray 1.95 A 2-843 [» ]
    3MSC X-ray 1.95 A 2-843 [» ]
    3MT7 X-ray 2.00 A 2-843 [» ]
    3MT8 X-ray 2.00 A 2-843 [» ]
    3MT9 X-ray 2.05 A 2-843 [» ]
    3MTA X-ray 2.23 A 2-843 [» ]
    3MTB X-ray 1.95 A 2-843 [» ]
    3MTD X-ray 2.10 A 2-843 [» ]
    3NC4 X-ray 2.07 A 3-843 [» ]
    3NP7 X-ray 2.05 A 2-843 [» ]
    3NP9 X-ray 2.00 A 2-843 [» ]
    3NPA X-ray 1.97 A 2-843 [» ]
    3S0J X-ray 2.00 A 2-843 [» ]
    3SYM X-ray 2.40 A 2-843 [» ]
    3SYR X-ray 2.40 A 2-843 [» ]
    3T3D X-ray 2.50 A 2-843 [» ]
    3T3E X-ray 2.15 A 2-843 [» ]
    3T3G X-ray 2.40 A 2-843 [» ]
    3T3H X-ray 2.60 A 2-843 [» ]
    3T3I X-ray 2.65 A 2-843 [» ]
    3ZCP X-ray 1.83 A 1-843 [» ]
    3ZCQ X-ray 2.15 A 1-843 [» ]
    3ZCR X-ray 2.07 A 1-843 [» ]
    3ZCS X-ray 2.03 A 1-843 [» ]
    3ZCT X-ray 2.00 A 1-843 [» ]
    3ZCU X-ray 2.05 A 1-843 [» ]
    3ZCV X-ray 1.83 A 1-843 [» ]
    4EJ2 X-ray 2.65 A 13-837 [» ]
    4EKE X-ray 2.60 A 13-837 [» ]
    4EKY X-ray 2.45 A 13-837 [» ]
    4EL0 X-ray 2.40 A 13-837 [» ]
    4EL5 X-ray 2.00 A 13-837 [» ]
    4GPB X-ray 2.30 A 2-843 [» ]
    4MRA X-ray 2.34 A 13-837 [» ]
    5GPB X-ray 2.30 A 2-843 [» ]
    6GPB X-ray 2.86 A 2-843 [» ]
    7GPB X-ray 2.90 A/B/C/D 2-843 [» ]
    8GPB X-ray 2.20 A 2-843 [» ]
    9GPB X-ray 2.90 A/B/C/D 2-843 [» ]
    ProteinModelPortali P00489.
    SMRi P00489. Positions 15-843.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-38240N.
    IntActi P00489. 2 interactions.
    MINTi MINT-6368963.

    Chemistry

    BindingDBi P00489.
    ChEMBLi CHEMBL4696.
    DrugBanki DB00131. Adenosine monophosphate.

    Protein family/group databases

    CAZyi GT35. Glycosyltransferase Family 35.

    Proteomic databases

    PRIDEi P00489.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100008972.

    Organism-specific databases

    CTDi 5837.

    Phylogenomic databases

    eggNOGi COG0058.
    HOGENOMi HOG000278444.
    HOVERGENi HBG006848.

    Enzyme and pathway databases

    BRENDAi 2.4.1.1. 1749.
    SABIO-RK P00489.

    Miscellaneous databases

    EvolutionaryTracei P00489.

    Family and domain databases

    InterProi IPR011833. Glycg_phsphrylas.
    IPR000811. Glyco_trans_35.
    [Graphical view ]
    PANTHERi PTHR11468. PTHR11468. 1 hit.
    Pfami PF00343. Phosphorylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000460. Pprylas_GlgP. 1 hit.
    TIGRFAMsi TIGR02093. P_ylase. 1 hit.
    PROSITEi PS00102. PHOSPHORYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPYGM_RABIT
    AccessioniPrimary (citable) accession number: P00489
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3