ID A0A3B6KPU0_WHEAT Unreviewed; 968 AA.
AC A0A3B6KPU0;
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};
GN ORFNames=CFC21_067736 {ECO:0000313|EMBL:KAF7061003.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5A02G395200.1};
RN [1] {ECO:0000313|EMBL:KAF7061003.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7061003.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5A02G395200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5A02G395200.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5A02G395200.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7061003.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7061003.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CM022223; KAF7061003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6KPU0; -.
DR SMR; A0A3B6KPU0; -.
DR STRING; 4565.A0A3B6KPU0; -.
DR EnsemblPlants; TraesCS5A02G395200.1; TraesCS5A02G395200.1; TraesCS5A02G395200.
DR Gramene; TraesCAD_scaffold_028097_01G000100.1; TraesCAD_scaffold_028097_01G000100.1; TraesCAD_scaffold_028097_01G000100.
DR Gramene; TraesCLE_scaffold_091711_01G000100.1; TraesCLE_scaffold_091711_01G000100.1; TraesCLE_scaffold_091711_01G000100.
DR Gramene; TraesCS5A02G395200.1; TraesCS5A02G395200.1; TraesCS5A02G395200.
DR Gramene; TraesKAR5A01G0359420.1; cds.TraesKAR5A01G0359420.1; TraesKAR5A01G0359420.
DR Gramene; TraesPAR_scaffold_020683_01G000100.1; TraesPAR_scaffold_020683_01G000100.1; TraesPAR_scaffold_020683_01G000100.
DR Gramene; TraesROB_scaffold_024036_01G000500.1; TraesROB_scaffold_024036_01G000500.1; TraesROB_scaffold_024036_01G000500.
DR OrthoDB; 5473321at2759; -.
DR Proteomes; UP000019116; Chromosome 5A.
DR Proteomes; UP000815260; Chromosome 5A.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 512..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 814
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 968 AA; 108522 MW; C7181E9C13DF5DFB CRC64;
MATASPPLAT PFRPLAVAGG SGGLVVGARA VVPPRRGRRG FVVRSVASDR EVRGPAPTEE
ELSAVLTSID SSAIASNIQH HADFTPLFSP EHSSPLKAYH ATAKSVFDSL ILNWNATYDY
YNKVNAKQAY YLSMEFLQGR ALTNAIGNLE LTGQYAEALK QLGQNLEDVA SQEPDPALGN
GGLGRLASCF LDSMATLNYP AWGYGLRYRY GLFKQIITKD GQEEVAENWL EMGNPWEIVR
NDVSYPLKFY GKVVEGTDGR KHWIGGENIK AVAHDVPIPG YKTKTTNNLR LWSTTVPSQN
FDLGAFNAGD HVKANEAHLN AEKICHVLYP GDESSEGKIL RLKQQYTLCS ASLQDIISRF
ESRAGDSLNW EDFPSKVAVQ MNDTHPTLCI PELMRILMDV KGLSWNESWS ITERTVAYTN
HTVLPEALEK WSLDIMQKLL PRHVEIIERI DEELMNTIVS KYGTADISLL KQKLKDMRIL
DNVDLPASVA KLFIKPKEKK GKLLVESLES IAEADEKTES EEEENILSET TEKKGESDSE
EAPDAEKEDP EYELDPFTKY DPQLPRVVRM ANLCVVGGHS VNGVAEIHSE IVKQDVFNSF
YEMWPTKFQN KTNGVTPRRW IRFCNPELST IISKWIGSDD WILNTDKLAG LKKFADDEDL
QSEWRTAKRN NKMKVVSLIR DKTGYVVSPD AMFDVQVKRI HEYKRQLLNI LGIIYRYKKM
KEMSAKDRIK SFVPRVCIFG GKAFATYVQA KRIVKFITDV AATVNYDPDI GDLLKVVFVP
DYNVSVAETL IPASELSQHI STAGMEASGT SNMKFAMNGC ILIGTLDGAN VEIREEVGEE
NFFLFGAHAP EIAGLRQERA EGKFVPDPRF EEVKEYVRSG IFGTGNYDEL MGSLEGNEGY
GRADYFLVGK DFPSYIECQE KVDEAYRDQK LWTRMSILNT AGSPKFSSDR TIHEYAKDIW
GISPVIMP
//
