ID B3IYE3_ORYSJ Unreviewed; 978 AA.
AC B3IYE3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 13-SEP-2023, entry version 74.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=pho1 {ECO:0000313|EMBL:BAG49328.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000313|EMBL:BAG49328.1};
RN [1] {ECO:0000313|EMBL:BAG49328.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18621947; DOI=10.1105/tpc.107.054007;
RA Satoh H., Shibahara K., Tokunaga T., Nishi A., Tasaki M., Hwang S.,
RA Okita T.W., Kaneko N., Fujita N., Yoshida M., Hosaka Y., Sato A.,
RA Utsumi Y., Ohdan T., Nakamura Y.;
RT "Mutation of the plastidial alpha-glucan phosphorylase gene in rice affects
RT the synthesis and structure of starch in the endosperm.";
RL Plant Cell 20:1833-1849(2008).
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|ARBA:ARBA00001275,
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB441692; BAG49328.1; -; Genomic_DNA.
DR AlphaFoldDB; B3IYE3; -.
DR SMR; B3IYE3; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR BRENDA; 2.4.1.1; 4460.
DR PlantReactome; R-OSA-9626305; Regulatory network of nutrient accumulation.
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:0005975; P:carbohydrate 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:SF28; ALPHA-GLUCAN PHOSPHORYLASE 1; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 2.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
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 824
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 978 AA; 109161 MW; 9DE06010000532A7 CRC64;
MATASAPLQL ATASRPLPVG VGCGGGGGGG LHVGGARGGG AAPARRRLAV RSVASDRGVQ
GSVSPEEEIS SVLNSIDSST IASNIKHHAE FTPVFSPEHF SPLKAYHATA KSVLDTLIMN
WNATYDYYDR TNVKQAYYLS MEFLQGRALT NAVGNLELTG QYAEALQQLG HSLEDVATQE
PDAALGNGGL GRLASCFLDS LATLNYPAWG YGLRYKHGLF KQIITKDGQE EVAENWLEMG
NPWEIVRTDV SYPVKFYGKV VEGTDGRMHW IGGENIKVVA HDIPIPGYKT KTTNNLRLWS
TTVPSQDFDL EAFNAGDHAS AYEAHLNAEK ICHVLYPGDE SPEGKVLRLK QQYTLCSASL
QDIIARFERR AGDSLSWEDF PSKVAVQMND THPTLCIPEL MRILIDVKGL SWNEAWSITE
RTVAYTNHTV LPEALEKWSL DIMQKLLPRH VEIIEKIDGE LMNIIISKYG TEDTSLLKKK
IKEMRILDNI DLPDSIAKLF VKPKEKKESP AKLKEKLLVK SLEPSVVVEE KTVSKVEINE
DSEEVEVDSE EVVEAENEDS EDELDPFVKS DPKLPRVVRM ANLCVVGGHS VNGVAAIHSE
IVKEDVFNSF YEMWPAKFQN KTNGVTPRRW IRFCNPELSA IISKWIGSDD WVLNTDKLAE
LKKFADDEDL QSEWRAAKKA NKVKVVSLIR EKTGYIVSPD AMFDVQVKRI HEYKRQLLNI
LGIVYRYKKM KEMSAKDRIN SFVPRVCIFG GKAFATYVQA KRIVKFITDV AATVNHDPEI
GDLLKVVFIP DYNVSVAEAL IPASELSQHI STAGMEASGT SNMKFAMNGC ILIGTLDGAN
VEIREEVGEE NFFLFGAEAH EIAGLRKERA QGKFVPDPRF EEVKRFVRSG VFGTYNYDDL
MGSLEGNEGY GRADYFLVGK DFPSYIECQE KVDKAYRDQK LWTRMSILNT ASSSKFNSDR
TIHEYAKDIW DIKPVILP
//
