ID F7FVH2_ORNAN Unreviewed; 842 AA.
AC F7FVH2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=PYGM {ECO:0000313|Ensembl:ENSOANP00000021628.2};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000021628.2, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000021628.2, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000021628.2,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000021628.2}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000021628.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|ARBA:ARBA00037413,
CC ECO:0000256|RuleBase:RU000587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00036074};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000256|ARBA:ARBA00036074};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR AlphaFoldDB; F7FVH2; -.
DR STRING; 9258.ENSOANP00000021628; -.
DR Ensembl; ENSOANT00000021631.3; ENSOANP00000021628.2; ENSOANG00000013714.3.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_0_3_1; -.
DR InParanoid; F7FVH2; -.
DR OMA; IYDINWR; -.
DR OrthoDB; 5473321at2759; -.
DR TreeFam; TF300309; -.
DR Proteomes; UP000002279; Chromosome 3.
DR Bgee; ENSOANG00000013714; Expressed in heart and 4 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 842 AA; 96951 MW; 52611A78CCCFF665 CRC64;
MSLPMSDHDK RKQISVRGLA GVENVSDLKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
RDHLVGRWIR TQQHYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK INNGWQMEEA
DDWLRYGNPW EKARPEFTLP VHFYGRVEHT DQGAKWVDTQ IVLAMPYDTP VPGYRNNTVN
TMRLWSAKAP NDFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKSSKFGCR DAVRTNFEAF PEKVAIQLND THPSLAIPEL MRVLVDVEKL
EWDKAWDVTV KTCAYTNHTV LPEALERWPV HLLETLLPRH LQIIYEINQR FLNRVAAAFP
GDMDRLRRMS LVEEGGVKRI NMAHLCIAGA HAVNGVARIH SEILKKTIFK DFYELEPHKF
QNKTNGITPR RWLVLCNPGL AEVIAERIGE EYISDLDQLR KLLAYVDDEG FIRDVAKVKQ
ENKLKFAAYL EKEYNVHINP NSLFDVQVKR IHEYKRQLLN CLHVITLYNR IKKDPNKFFV
PRTVMIGGKA APGYHMAKMI IKLITSIGDV VNNDPVVGDR LKMIFLENYR VSLAEKVIPA
SDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENFF IFGMRVEDVD
RLDQKGYNAQ EFYDSLPELR QVIEQLSSGF FSPKQPDLFK DIVNMLMHHD RFKVFADFKA
YIQCQEKVSA LYKNPREWTR MVIRNIATSG KFSSDRTIAQ YAREIWGVEP SHQRLAAPDE
HF
//