ID   PHSL1_SOLTU             Reviewed;         966 AA.
AC   P04045;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase L-1 isozyme, chloroplastic/amyloplastic;
DE            EC=2.4.1.1;
DE   AltName: Full=Starch phosphorylase L-1;
DE   Flags: Precursor;
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].
RX   PubMed=2481677; DOI=10.1093/oxfordjournals.jbchem.a122918;
RA   Nakano K., Mori H., Fukui T.;
RT   "Molecular cloning of cDNA encoding potato amyloplast alpha-glucan
RT   phosphorylase and the structure of its transit peptide.";
RL   J. Biochem. 106:691-695(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Kennebec;
RX   PubMed=1703627; DOI=10.1007/bf00259448;
RA   Camirand A., St Pierre B., Marineau C., Brisson N.;
RT   "Occurrence of a copia-like transposable element in one of the introns of
RT   the potato starch phosphorylase gene.";
RL   Mol. Gen. Genet. 224:33-39(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 51-966.
RX   PubMed=3722153; DOI=10.1016/s0021-9258(19)83900-5;
RA   Nakano K., Fukui T.;
RT   "The complete amino acid sequence of potato alpha-glucan phosphorylase.";
RL   J. Biol. Chem. 261:8230-8236(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 51-131.
RX   PubMed=7410423; DOI=10.1016/s0021-9258(19)70555-9;
RA   Nakano K., Fukui T., Matsubara H.;
RT   "Structural basis for the difference of the regulatory properties between
RT   potato and rabbit muscle phosphorylases. The NH2-terminal sequence of the
RT   potato enzyme.";
RL   J. Biol. Chem. 255:9255-9261(1980).
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       P04045; P04045: -; NbExp=2; IntAct=EBI-780963, EBI-780963;
CC       P04045; P53535: STP-1; NbExp=2; IntAct=EBI-780963, EBI-780968;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast.
CC   -!- TISSUE SPECIFICITY: Tuber.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; D00520; BAA00407.1; -; mRNA.
DR   EMBL; X52385; CAA36612.1; -; mRNA.
DR   PIR; JU0130; PHPOAG.
DR   RefSeq; NP_001275215.1; NM_001288286.1.
DR   AlphaFoldDB; P04045; -.
DR   SMR; P04045; -.
DR   IntAct; P04045; 1.
DR   STRING; 4113.PGSC0003DMT400020094; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; P04045; -.
DR   ProMEX; P04045; -.
DR   GeneID; 102596766; -.
DR   KEGG; sot:102596766; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   OrthoDB; 240595at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P04045; 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:0042802; F:identical protein binding; IPI:IntAct.
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   Direct protein sequencing; Glycosyltransferase; Plastid;
KW   Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:3722153,
FT                   ECO:0000269|PubMed:7410423"
FT   CHAIN           51..966
FT                   /note="Alpha-1,4 glucan phosphorylase L-1 isozyme,
FT                   chloroplastic/amyloplastic"
FT                   /id="PRO_0000012292"
FT   MOD_RES         812
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        159
FT                   /note="A -> D (in Ref. 2; CAA36612)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   966 AA;  109506 MW;  A7758860A790793A CRC64;
     MATANGAHLF NHYSSNSRFI HFTSRNTSSK LFLTKTSHFR RPKRCFHVNN TLSEKIHHPI
     TEQGGESDLS SFAPDAASIT SSIKYHAEFT PVFSPERFEL PKAFFATAQS VRDSLLINWN
     ATYDIYEKLN MKQAYYLSME FLQGRALLNA IGNLELTGAF AEALKNLGHN LENVASQEPD
     AALGNGGLGR LASCFLDSLA TLNYPAWGYG LRYKYGLFKQ RITKDGQEEV AEDWLEIGSP
     WEVVRNDVSY PIKFYGKVST GSDGKRYWIG GEDIKAVAYD VPIPGYKTRT TISLRLWSTQ
     VPSADFDLSA FNAGEHTKAC EAQANAEKIC YILYPGDESE EGKILRLKQQ YTLCSASLQD
     IISRFERRSG DRIKWEEFPE KVAVQMNDTH PTLCIPELMR ILIDLKGLNW NEAWNITQRT
     VAYTNHTVLP EALEKWSYEL MQKLLPRHVE IIEAIDEELV HEIVLKYGSM DLNKLEEKLT
     TMRILENFDL PSSVAELFIK PEISVDDDTE TVEVHDKVEA SDKVVTNDED DTGKKTSVKI
     EAAAEKDIDK KTPVSPEPAV IPPKKVRMAN LCVVGGHAVN GVAEIHSEIV KEEVFNDFYE
     LWPEKFQNKT NGVTPRRWIR FCNPPLSAII TKWTGTEDWV LKTEKLAELQ KFADNEDLQN
     EWREAKRSNK IKVVSFLKEK TGYSVVPDAM FDIQVKRIHE YKRQLLNIFG IVYRYKKMKE
     MTAAERKTNF VPRVCIFGGK AFATYVQAKR IVKFITDVGA TINHDPEIGD LLKVVFVPDY
     NVSVAELLIP ASDLSEHIST AGMEASGTSN MKFAMNGCIQ IGTLDGANVE IREEVGEENF
     FLFGAQAHEI AGLRKERADG KFVPDERFEE VKEFVRSGAF GSYNYDDLIG SLEGNEGFGR
     ADYFLVGKDF PSYIECQEKV DEAYRDQKRW TTMSILNTAG SYKFSSDRTI HEYAKDIWNI
     EAVEIA