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Database: UniProt
Entry: F6ZD04_HORSE
LinkDB: F6ZD04_HORSE
Original site: F6ZD04_HORSE 
ID   F6ZD04_HORSE            Unreviewed;       843 AA.
AC   F6ZD04;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   27-MAR-2024, entry version 67.
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:ENSECAP00000020068.2,
GN   ECO:0000313|VGNC:VGNC:22061};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000020068.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000020068.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000020068.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000020068.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000020068.2};
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   AlphaFoldDB; F6ZD04; -.
DR   SMR; F6ZD04; -.
DR   STRING; 9796.ENSECAP00000020068; -.
DR   PaxDb; 9796-ENSECAP00000020068; -.
DR   Ensembl; ENSECAT00000024169.4; ENSECAP00000020068.2; ENSECAG00000022048.4.
DR   VGNC; VGNC:22061; PYGB.
DR   GeneTree; ENSGT00950000183148; -.
DR   HOGENOM; CLU_010198_1_1_1; -.
DR   InParanoid; F6ZD04; -.
DR   OMA; WLKQANP; -.
DR   OrthoDB; 5473321at2759; -.
DR   TreeFam; TF300309; -.
DR   Proteomes; UP000002281; Chromosome 22.
DR   Bgee; ENSECAG00000022048; Expressed in articular cartilage of joint and 23 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: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   1: Evidence at protein level;
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   Proteomics identification {ECO:0007829|PeptideAtlas:F6ZD04};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
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   843 AA;  96415 MW;  FAF48533A2E84241 CRC64;
     MAKPLTDSEK RKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV
     RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQNACD EAIYQLGLDL
     EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
     DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PEGVRWLDTQ VVLAMPYDTP VPGYKNNTVN
     TMRLWSAKAP NDFKLHDFNV GGYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDIIR RFKSSKFGCR DPVRTCFETF PDKVAIQLND THPALAIPEL MRILVDVEKV
     DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LDIIYAINQR HLDHVAALFP
     GDVDRLRRMS VIEEGDCKRI NMAHLCVIGT HAVNGVARIH SEIVKQSVFK DFYELEPEKF
     QNKTNGITPR RWLLLCNPGL ADTIVEKIGE GFLTDLSQLK KLLPLASDEA LIRDVAKVKQ
     ENKLKFSAFL EKEYKVKINP SSMFDVHVKR IHEYKRQLLN CLHVVTLYNR IKKDPARPFV
     PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LKVIFLENYR VSLAEKVIPA
     ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGAENLF IFGLRVEDVE
     ALDQKGYHAR EYYDRLPELR QAVDQISSGF FSPKEPDCFK DVVNMLLNHD RFKVFADYEA
     YMACQAQVDQ LYRNPKEWTK KVIKNIACSG KFSSDRTITE YARDIWGVEP SDLQIPPPNL
     PKD
//
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