ID   PHSL2_SOLTU             Reviewed;         974 AA.
AC   P53535;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic;
DE            EC=2.4.1.1;
DE   AltName: Full=Starch phosphorylase L-2;
DE   Flags: Precursor;
GN   Name=STP-1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   PubMed=7894019; DOI=10.1007/bf00019322;
RA   Sonnewald U., Basner A., Greve B., Steup M.;
RT   "A second L-type isozyme of potato glucan phosphorylase: cloning, antisense
RT   inhibition and expression analysis.";
RL   Plant Mol. Biol. 27:567-576(1995).
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   -!- INTERACTION:
CC       P53535; P04045; NbExp=2; IntAct=EBI-780968, EBI-780963;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC   -!- TISSUE SPECIFICITY: Leaves.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; X73684; CAA52036.1; -; mRNA.
DR   PIR; S53489; S34189.
DR   RefSeq; NP_001275128.1; NM_001288199.1.
DR   AlphaFoldDB; P53535; -.
DR   SMR; P53535; -.
DR   IntAct; P53535; 1.
DR   STRING; 4113.PGSC0003DMT400072963; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; P53535; -.
DR   GeneID; 102603391; -.
DR   KEGG; sot:102603391; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   InParanoid; P53535; -.
DR   OrthoDB; 240595at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P53535; baseline and differential.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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   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   1: Evidence at protein level;
KW   Allosteric enzyme; Amyloplast; Carbohydrate metabolism; Chloroplast;
KW   Glycosyltransferase; Plastid; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..81
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           82..974
FT                   /note="Alpha-1,4 glucan phosphorylase L-2 isozyme,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000012293"
FT   REGION          509..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..528
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..551
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         820
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   974 AA;  110700 MW;  5EF8A23C237463D8 CRC64;
     MATFAVSGLN SISSISSFNN NFRSKNSNIL LSRRRILLFS FRRRRRSFSV SSVASDQKQK
     TKDSSSDEGF TLDVFQPDST SVLSSIKYHA EFTPSFSPEK FELPKAYYAT AESVRDTLII
     NWNATYEFYE KMNVKQAYYL SMEFLQGRAL LNAIGNLGLT GPYADALTKL GYSLEDVARQ
     EPDAALGNGG LGRLASCFLD SMATLNYPAW GYGLRYQYGL FKQLITKDGQ EEVAENWLEM
     GNPWEIVRND ISYPVKFYGK VIEGADGRKE WAGGEDITAV AYDVPIPGYK TKTTINLRLW
     TTKLAAEAFD LYAFNNGDHA KAYEAQKKAE KICYVLYPGD ESLEGKTLRL KQQYTLCSAS
     LQDIIARFEK RSGNAVNWDQ FPEKVAVQMN DTHPTLCIPE LLRILMDVKG LSWKQAWEIT
     QRTVAYTNHT VLPEALEKWS FTLLGELLPR HVEIIAMIDE ELLHTILAEY GTEDLDLLQE
     KLNQMRILDN VEIPSSVLEL LIKAEESAAD VEKAADEEQE EEGKDDSKDE ETEAVKAETT
     NEEEETEVKK VEVEDSQAKI KRIFGPHPNK PQVVHMANLC VVSGHAVNGV AEIHSEIVKD
     EVFNEFYKLW PEKFQNKTNG VTPRRWLSFC NPELSEIITK WTGSDDWLVN TEKLAELRKF
     ADNEELQSEW RKAKGNNKMK IVSLIKEKTG YVVSPDAMFD VQIKRIHEYK RQLLNIFGIV
     YRYKKMKEMS PEERKEKFVP RVCIFGGKAF ATYVQAKRIV KFITDVGETV NHDPEIGDLL
     KVVFVPDYNV SVAEVLIPGS ELSQHISTAG MEASGTSNMK FSMNGCLLIG TLDGANVEIR
     EEVGEDNFFL FGAQAHEIAG LRKERAEGKF VPDPRFEEVK AFIRTGVFGT YNYEELMGSL
     EGNEGYGRAD YFLVGKDFPD YIECQDKVDE AYRDQKKWTK MSILNTAGSF KFSSDRTIHQ
     YARDIWRIEP VELP