ID   A0A3B3QAV8_9TELE        Unreviewed;       842 AA.
AC   A0A3B3QAV8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000003303.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000003303.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   AlphaFoldDB; A0A3B3QAV8; -.
DR   STRING; 1676925.ENSPKIP00000003303; -.
DR   Ensembl; ENSPKIT00000027262.1; ENSPKIP00000003303.1; ENSPKIG00000020850.1.
DR   GeneTree; ENSGT00950000183148; -.
DR   OrthoDB; 5473321at2759; -.
DR   Proteomes; UP000261540; Unplaced.
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:SF11; ALPHA-1,4 GLUCAN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 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   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;  97071 MW;  876166D1628ABA6E CRC64;
     MSRPLSDQEK RKQISVRGLA GVENVTEIKS SFNRHLHFTL VKDRNVATRR DYYFALANTV
     RDHLVGRWIR TQQYYYERDP KRVYYLSLEF YMGRTLQNTM VNLALENACD EATYQLGLDM
     EELEDMEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVSGWQVEEA
     DDWLRYGNPW EKARPEYMRP VHFYGRTEHH PDGVKWVDTQ VVLALPYDTP VPGYRNNVVN
     TMRLWSAKAP CEFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDIIR RYKTSKFGSK EEVRTDLSGL PDKVAIQLND THPSLAIPEL MRILVDDEKQ
     SWDKAWDICV RSCAYTNHTV LPEALERWPI DLFQRLLPRH LEIIYEINRR HLERISSLYP
     GDMDRMRRMS LIEEGDQKRV NMAHLCIVGS HAVNGVARIH SDILKATVFK DFYEMDPLKF
     QNKTNGITPR RWLVMCNPGL AEIIAERIGE EFIHDLDQLK KLLDFVNDEA FIRDIAKVKQ
     ENKLKFAVHL EEHYKVKINP NSIFDLQVKR IHEYKRQLLN CLHIITFYNR IKKDPNKHWV
     PRTIMIGGKA APGYHTAKMI IRLITAIGEI VNNDPVVGDR LKVIFLENYR VTLAEKAIPA
     ADLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVE
     ALDRKGYNAG EYYSRIPELK QAIDQIAGGF FSPSQPDLFK DIVDLLMHHD RFKVFADYED
     YMKCQDKVGA LYKNPKEWTR KVIHNIAGCG KFSSDRTIGQ YAREIWGIEP TLEKIPGPDE
     KR
//