ID A0A3Q2ZV46_KRYMA Unreviewed; 842 AA.
AC A0A3Q2ZV46;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000007746.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000007746.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSKMAP00000007746.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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 -!- SUBUNIT: Homodimer. Homotetramer; to form the enzymatically active
CC phosphorylase A. {ECO:0000256|ARBA:ARBA00046356}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR RefSeq; XP_017282553.1; XM_017427064.1.
DR AlphaFoldDB; A0A3Q2ZV46; -.
DR STRING; 37003.ENSKMAP00000007746; -.
DR Ensembl; ENSKMAT00000007869.1; ENSKMAP00000007746.1; ENSKMAG00000005773.1.
DR GeneID; 108242298; -.
DR KEGG; kmr:108242298; -.
DR GeneTree; ENSGT00950000183148; -.
DR OMA; DLDPQKF; -.
DR OrthoDB; 9215500at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0052576; P:carbohydrate storage; IEA:Ensembl.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:TreeGrafter.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000005; Alpha-1,4 glucan phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000153; Alpha-1,4 glucan phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000197; Alpha-1,4 glucan 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:SF32; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
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; 96824 MW; 5A61EFC7A827BFF0 CRC64;
MAKPLTDQDK RKQISVRGLA GVENVADLKT NFNRHLHFTL VKDRNVATKR DYYFALANTV
RDHLVGRWIR TQQHYYEKDP KRVYYLSLEF YMGRALQNTM VNLGLENACD EATYQLGLDM
EELQDIEEDA GLGNGGLGRL AACFLDSMAS LGLAAYGYGI RYEFGIFNQK IMNGWQVEEA
DDWLRYGNPW EKARPEYMRP VHFYGRVEHT AEGVKWVDTQ VVLALPYDTP VPGYRNNIVN
TMRLWSAKAP CEFNLKDFNV GGYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKASKFGST EFVRMDLSTM PDKVAIQLND THPALAIPEL MRLLVDNEKL
TWEKAWDIVV RTCAYTNHTV LPEALERWPV DLFQNLLPRH LEIIYEINRR HMERIGKLYP
GDFDRMRRMS LIEEGDVKKI NMAHLCIVGS HAVNGVARIH SEIIKDTVFK DFYDVDPQKF
QNKTNGITPR RWLVMCNPGL AEIIAERIGE DYIRDLDQLK KLLNFVNDDS FIRDVAKVKQ
ENKLKFSAHL EEQYKVKINP NSMFDVQVKR IHEYKRQLLN CLHIITLYNR IRKEPSKPWT
PRTIMIGGKA APGYHTAKMI IKLITSIGDI VNNDPVVGDR LKVIFLENYR VTLAEKIIPA
SDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEQNLF IFGMRVHEVE
ALDKKGYDAV SYYNRIPELK QAIDQISGGF FSPAQPGLFK DLVNMLMNHD RFKVFADYEE
YIKCQDKVSA LYKNPKEWTK KVIYNIAGCG KFSSDRTISQ YAREIWGIEP SLEKIAAPDD
PR
//
