ID   PHSL_IPOBA              Reviewed;         955 AA.
AC   P27598;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase L isozyme, chloroplastic/amyloplastic;
DE            EC=2.4.1.1;
DE   AltName: Full=Starch phosphorylase L;
DE   Flags: Precursor;
OS   Ipomoea batatas (Sweet potato) (Convolvulus batatas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX   NCBI_TaxID=4120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668119; DOI=10.1104/pp.95.4.1250;
RA   Lin C.T., Yeh K.W., Lee P.D., Su J.C.;
RT   "Primary structure of sweet potato starch phosphorylase deduced from its
RT   cDNA sequence.";
RL   Plant Physiol. 95:1250-1253(1991).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Enzymes from different sources differ in their
CC       regulatory mechanisms and in their natural substrates. However, all
CC       known phosphorylases share catalytic and structural properties.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; M64362; AAA63271.1; -; mRNA.
DR   PIR; T10947; T10947.
DR   AlphaFoldDB; P27598; -.
DR   SMR; P27598; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   PANTHER; PTHR11468; PTHR11468; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02093; P_ylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Amyloplast; Carbohydrate metabolism; Chloroplast;
KW   Glycosyltransferase; Plastid; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..43
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..955
FT                   /note="Alpha-1,4 glucan phosphorylase L isozyme,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000012291"
FT   REGION          522..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         801
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   955 AA;  108520 MW;  CCDB7CD5628A662A CRC64;
     MSRLSGITPR ARDDRSQFQN PRLEIAVPDR TAGLQRTKRT LLVKCVLDET KQTIQHVVTE
     KNEGTLLDAA SIASSIKYHA EFSPAFSPER FELPKAYFAT AQSVRDALIV NWNATYDYYE
     KLNMKQAYYL SMEFLQGRAL LNAIGNLELT GEYAEALNKL GHNLENVASK EPDAALGNGG
     LGRLASCFLD SLATLNYPAW GYGLRYKYGL FKQRITKDGQ EEVAEDWLEL GNPWEIIRMD
     VSYPVKFFGK VITGSDGKKH WIGGEDILAV AYDVPIPGYK TRTTISLRLW STKVPSEDFD
     LYSFNAGEHT KACEAQANAE KICYILYPGD ESIEGKILRL KQQYTLCSAS LQDIIARFER
     RSGEYVKWEE FPEKVAVQMN DTHPTLCIPE LIRILIDLKG LSWKEAWNIT QRTVAYTNHT
     VLPEALEKWS YELMEKLLPR HIEIIEMIDE QLINEIVSEY GTSDLDMLEK KLNDMRILEN
     FDIPSSIANL FTKPKETSIV DPSEEVEVSG KVVTESVEVS DKVVTESEKD ELEEKDTELE
     KDEDPVPAPI PPKMVRMANL CVVGGHAVNG VAEIHSDIVK EDVFNDFYQL WPEKFQNKTN
     GVTPRRWIRF CNPALSNIIT KWIGTEDWVL NTEKLAELRK FADNEDLQIE WRAAKRSNKV
     KVASFLKERT GYSVSPNAMF DIQVKRIHEY KRQLLNILGI VYRYKQMKEM SAREREAKFV
     PRVCIFGGKA FATYVQAKRI AKFITDVGAT INHDPEIGDL LKVIFVPDYN VSAAELLIPA
     SGLSQHISTA GMEASGQSNM KFAMNGCILI GTLDGANVEI RQEVGEENFF LFGAEAHEIA
     GLRKERAEGK FVPDERFEEV KEFIKRGVFG SNTYDELLGS LEGNEGFGRG DYFLVGKDFP
     SYIECQEKVD EAYRDQKIWT RMSILNTAGS YKFSSDRTIH EYAKDIWNIQ PVVFP