ID A0A2T7C0W5_9POAL Unreviewed; 985 AA.
AC A0A2T7C0W5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=GQ55_9G078500 {ECO:0000313|EMBL:PUZ36947.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ36947.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ36947.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-2018) 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; CM009757; PUZ36947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7C0W5; -.
DR STRING; 1504633.A0A2T7C0W5; -.
DR EnsemblPlants; PUZ36947; PUZ36947; GQ55_9G078500.
DR Gramene; PUZ36947; PUZ36947; GQ55_9G078500.
DR Proteomes; UP000244336; Chromosome 9.
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 Reference proteome {ECO:0000313|Proteomes:UP000244336};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 536..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..571
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 831
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 985 AA; 110303 MW; 030D9A41E775F3D5 CRC64;
MATNASPPLQ LATAFRPLAS ASAAGGGGGG VGLLAGGGVA AGRGRERTQR RVVAARSVAS
DRDVQGPVSP EEGLPSVLNS MDSCAIASNI KHHAEFKPLF APEHFSPLNA YHATAKSVFD
ALLINWNATY NYYNKMNVKQ AYYLSMEFLQ GRALTNAIGN LELTGEYAEA LKQLGHNLED
VASQEPDAAL GNGGLGRLAS CFLDSLATLN YPAWGYGLRY KYGLFKQLIT KDGQEEVAEN
WLEMGYPWEI VRNDLSYPVK FYGKVVEGTD GRKHWIGGEN IKAVAYDVPI PGYKTRVTNN
LRLWSTTVPA QDFDLGAFNA GDHTKAYEAH LNAEKICHVL YPGDESPEGK VLRLKQQYTL
CSASLQDIIA RFEGRAGDSL NWEDFPSKVA VQMNDTHPTL CIPELMRILI DFKGLSWDEA
WRITERTVAY TNHTVLPEAL EKWSLDIMQK LLPRHVEIIE KIDEELMNNI VSKYGTSDTA
LLKKKLKEMR ILDNVDLPAS IAQLFVKPKE KKKSPTKSKK KLLVKSLETI AEVEEKTKLE
EEEAEVLSET EEEKVESEEV EAEEEDSEDG LDPFVKSDPK LPRVVRMANL CVVGGHSVNG
VAEIHSEIVK QDVFNSFYEM WPTKFQNKTN GVTPRRWIRF CNPELSTIIS KWIGSDDWVL
NTDKLAELKK FADNEDLHSE WRAAKLANKM KVVSLIRDKT GYIVSPDAMF DVQVKRIHEY
KRQLLNILGI IYRYKKMKEM SAEERVKRFV PRVCIFGGKA FATYIQAKRI VKFITDVAAT
VNHDSDIGDL LKVIFVPDYN VSVAEALIPA SELSQHISTA GMEASGTSNM KFAMNGCILI
GTLDGANVEI REEVGEENFF LFGAEAHEIV GLRKERAEGK FVPDPRFQEV KEFVRSGVFG
TYNYDELMGS LEGNEGYGRA DYFLVGKDFP SYIECQEKVD EAYRDQKLWT KMSILNTAGS
SKFSSDRTIH EYAKDIWDIS PVTLP
//
