ID   A0A3Q1C2L4_AMPOC        Unreviewed;       810 AA.
AC   A0A3Q1C2L4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000020910.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000020910.1}
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|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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   AlphaFoldDB; A0A3Q1C2L4; -.
DR   Ensembl; ENSAOCT00000011858.1; ENSAOCP00000020910.1; ENSAOCG00000005360.1.
DR   GeneTree; ENSGT00950000183148; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:SF26; GLYCOGEN PHOSPHORYLASE, LIVER 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}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         679
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   810 AA;  93025 MW;  F4E99B480F2450E1 CRC64;
     MATPLTDQEK RKQISIRGIA GVENVAELKK GFNRHLHFTL VKDRNIATPR DYYFALAHTV
     RDHLVGRWIR TQQFYYEADP KRVYYLSLEF YMGRTLQNTM INLGLQNACD ESIYQLGLDM
     EELEEMEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA
     DDWLRHGNPW EKARPEYMLP VHFYGRVEET RDGSKWVDTQ VVLAMPYDTP IPGYMNNTVN
     TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDIIR RFKTTKKGSP GRTSFETFPD KVAIQLNDTH PAMAIPELMR IFVDIEKLDW
     ETAWDLTRRT FAYTNHTVLP EALERWPVEL LENLLPRHLQ IIYQINQVHL DRIAALFPKD
     MDKLRKMSLI EEDGCKRVNM AHLCIVGSHA VNGVAEIHSN IIKTEVFRDF SDLEPQKFQN
     KTNGITPRRW LLLCNPGLAE LIAEVIGEEY VKDLGQLQKL NDFAEDAAFI RDVSKVKQDN
     KVKFAQYLEK EYRVKINPSS MFDVHVKRIH EYKRQVLNCL HIITMYNRIR KNPSAPFVPR
     TVIIGGKAAP GYHMAKMIIK LITSVADVVN NDPVVGNKLK VIFLENYRVS LAEKVIPATD
     LSEQISTAGT EASGTGNMKF MLNGALTIGT MDGANVEMAE EAGEENLFIF GMRVEDVAEM
     DKKGYDAMSY YKKIPELKQV MDQITSGFFS PKNPELFKDL TNMLFKHDRD RTITEYATEV
     WGVEPTDLKI PPPNEPREAI EETARALKKM
//