ID A0A2U1P889_ARTAN Unreviewed; 989 AA.
AC A0A2U1P889;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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_AA182610 {ECO:0000313|EMBL:PWA81973.1};
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:PWA81973.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA81973.1, 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:PWA81973.1};
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|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:PWA81973.1}.
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DR EMBL; PKPP01001526; PWA81973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1P889; -.
DR STRING; 35608.A0A2U1P889; -.
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: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; 3.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468:SF27; ALPHA-1,4 GLUCAN PHOSPHORYLASE L-2 ISOZYME, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 3.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 2.
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 REGION 517..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 835
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 989 AA; 112883 MW; 8429B217E385A7D3 CRC64;
MKFERVTMAA LSSSTYISKS SINDFSFTNN KHSKTFFFLN KKLHSRPRNL SLNNALSVNQ
QLFSLQQETR DSDNGTLVPD SESVISSIKY HAEFTPSFSP EKFELPKAFY ATAESVRDKL
IVNWNATYAY HEEMNVKQAY YLSMEFLQGR ALLNAIGNLE LSGAYAEALT KLGHDLEDVA
KQEPDAALGN GGLGRLASCF LDSLATLNYP AWGYGLRYKY GLFKQLITKD GQEEVAESWL
EMGNPWEIPR NDVSYPIKFY GEVVNGPDGR KEWVGGENIT AVAYDVPIPG YKTKTTINLR
LWSTKVAPEY FDLNAFNSGD HPKAYEALKR AEKICYILYP GDESHEGKTL RLKQQYTLCS
ASLQDIIARF ERRSGEALDW NKFPEKVAVQ MNDTHPTLCI PELLRILIDY KGLSWKEAWE
ITQKTVAYTN HTVLPEALEK WSLNLLQQLL PRHVELIEMI DKELIDTIIA EYGIKDLELV
KEKLKQMRVL DNVELPASVL EVLVQPEETP IVDLVKEEES TEEGSEEVTE ATSEDDELKV
KEPKEVKIIP KVTFETDPNQ PKMVRMANLC VVGGHAVNGV AEIHSEIVKN EVFNDFYKLW
PEKFQNKTNG VTPRRWISFC NPELSKIITK WTGTEDWVLN TEKLDELRNF ADNEDLQSEW
RKAKRINKEK MVSFLKEKTG YLVSPDAMFD VQVKRIHEYK RQLLNILGIV YRYKKMKEMS
AEERKENFVP RVCVFGGKAF ATYVQAKRIV KFITDVGATV NHDPDIGDLL KVVFVPDYNV
TVAEVLIPGS DLSQHIRYTS ISNLQFFFSL YGFDNWCPLI ISTAGMEASG TSNMKFAMNG
CIQIGTLDGA NVEIRQEVGE ENFFLFGAEA HEIAGLRKER SKGKFVPDPR FEEVKEYVRS
GVFGPYNYNE LMGSLEGNEG YGRADYFLVG KDFPAYIECQ DEVDKAYRDQ KKWTKMSILN
TAGSHKFSSD RTIHQYARDI WTIEPLVLP
//
