ID A0A2U1QDK0_ARTAN Unreviewed; 891 AA.
AC A0A2U1QDK0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CTI12_AA044220 {ECO:0000313|EMBL:PWA96052.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA96052.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA96052.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA96052.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWA96052.1}.
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DR EMBL; PKPP01000202; PWA96052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1QDK0; -.
DR STRING; 35608.A0A2U1QDK0; -.
DR Proteomes; UP000245207; Unassembled WGS sequence.
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:SF30; 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 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:UP000245207};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 742
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 891 AA; 101834 MW; 67C6F452556F64DA CRC64;
MGLLQMITKV LKDYKFEIPF IQFDEKSNLF VIKIVVSEKN GDGVKDNERL LKMLSGVVVM
REVGYDGNGG TKMFDLMDGF LRNDPMSLQK DVLHHVEYTV ARSRFSFDDF EAYQALSHSV
RDRLIERWHD TQQHFKKKDP KRLYFLSLEF LMGRSLSNSV INLGIRDQCA EAVNQLGFEY
EVLAEQEGDA ALGNGGLARL SACQMDSLAT LDYPAWGYGL RYQYGLFRQI ILDGFQHEQP
DYWLNFGNPW EIERVHVSYP VKFYGTVKDE DVNGKKCKVW IPKETVEAVA YDNPIPGYGT
RNTINLRLWA AKPSDANDIQ ESYNTGDYIN AIVNRQKAEI ISNVLYPDDR SYQGKELRLK
QQYFFVSASL QDIIRRFKDV HGNFDDFPDK VALQLNDTHP SISIAELMRV LLDEEHLGWK
RSWNIVSKVF SFTTHTVLPE ALEKVPADLL ENVLPRHLQI IYEINHAFME ELKKKIGQDY
ARLSRMSIVE EGAVKNIRVA NLSVYCSHTV NGVSRAHSEL IKTRVFTDFY ELWPEKFQYK
TNGVTQRRWI VVSNPSLCSL ITKWLGTESW IRNIDLLARL REYATNSDLQ QEWRMVKKIN
KMRLAEYIET MSGVKVSVDA MFDVQIKRIH AYKRQLLNIL GVIHRYDCIK NMDENERKNV
VPRVCIIGGK APPGYEIAKK IIKLCHAVAE TINNDSDVGD LLKLVFIPDY NVSVAELVIP
GSDLSQHIST AGHEASGTGS MKFLMNGCLL LATDDGSTNE IIEEIGAENM FIFGAKINEV
PALREKDSNV KAPLQFARVV RMVRDGYFGY KDYFNSLCDT VENGKDFYLV GSDFASYLEA
QAAADKAYVD KDKWTEMSIL CTAGSGRFSS DRTIEDYAAQ TWGIEPCKCP F
//
