ID W5PB77_SHEEP Unreviewed; 844 AA.
AC W5PB77;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=PYGB {ECO:0000313|Ensembl:ENSOARP00000007688.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000007688.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000007688.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000007688.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000007688.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|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|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC enzymatically active phosphorylase A. {ECO:0000256|ARBA:ARBA00038533}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; AMGL01025073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5PB77; -.
DR SMR; W5PB77; -.
DR Ensembl; ENSOART00000007803.1; ENSOARP00000007688.1; ENSOARG00000007168.1.
DR HOGENOM; CLU_010198_1_1_1; -.
DR OMA; WLKQANP; -.
DR Proteomes; UP000002356; Chromosome 13.
DR Bgee; ENSOARG00000007168; Expressed in heart right ventricle and 53 other cell types or tissues.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
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:SF29; GLYCOGEN PHOSPHORYLASE, BRAIN 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:UP000002356};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 682
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 844 AA; 95720 MW; 854C17C6A286047B CRC64;
AEAKPLTDGE RRKQISVRGL AGLGDVAEVR KSFNRHLHFT LVKDRNVATR RDYYLALAHT
VRDHLVGRWI RTQQRYYERD PKRIYYLSLE FYMGRTLQNT MVNLGLQNAC DEAIYQLGLD
LEELEEIEED AGLGNGGLGR LAACFLDSMA TLGLAAYGYG IRYEFGIFNQ KIVNGWQVAS
PPSWALVGGP GQEHQVLEEH GAGPGGHTRR VPPAQRWQEG QVVLAMPYDT PVPGYKNDTV
NTMRLWSAKA PNDFKLHDFN VGGYIEAVLD RNLAENISRV LYPNDNFFEG KELRLKQEYF
VVAATLQDII RRFKSSKFGC RDPVRTSFET FPDKVAIQLN DTHPALAIPE LMRILVDVEK
VDWGKAWEIT KKTCAYTNHT VLPEALERWP VSMFEKLLPR HLDIIYAINQ RHLDHVAALF
PGDVDRLRRM SVIEEGDCKR INMAHLCVIG SHAVNGVARI HSEIVRQSVF KDFYELEPEK
FQNKTNGITP RRWLLLCNPE LAETILARIG EDFLTDLSQL KKLLPLVGDE ALIRDVAQVK
QENKVKFSAF LEKQYGVKVN PSSMFDVHVK RIHEYKRQLL NCLHVVTLYN RIKKDPTQAF
VPRTVMIGGK AAPGYHMAKK IIKLVTSIGD IVNHDPIVGD RLKVIFLENY RVSLAEKVIP
AADLSQQIST AGTEASGTGN MKFMLNGALT IGTMDGANVE MAEEAGAENL FIFGLRVEDV
EALDRKGYNA HEYYNRLPEL QQAVDQINSG FFSPREPDCF KDVVNMLLNH DRFKVFADYE
AYVACQAQVD QLYRNPKEWT KKVIRNIACS GKFSSDRTIT EYARDIWGAE PPALQTPPPS
LPRD
//
