ID   PHSH_SOLTU              Reviewed;         838 AA.
AC   P32811;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Alpha-glucan phosphorylase, H isozyme;
DE            EC=2.4.1.1;
DE   AltName: Full=Starch phosphorylase H;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1917968; DOI=10.1016/s0021-9258(18)55082-1;
RA   Mori H., Tanizawa K., Fukui T.;
RT   "Potato tuber type H phosphorylase isozyme. Molecular cloning, nucleotide
RT   sequence, and expression of a full-length cDNA in Escherichia coli.";
RL   J. Biol. Chem. 266:18446-18453(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: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; M69038; AAA33809.1; -; mRNA.
DR   PIR; A40995; A40995.
DR   RefSeq; NP_001275118.1; NM_001288189.1.
DR   AlphaFoldDB; P32811; -.
DR   SMR; P32811; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; P32811; -.
DR   GeneID; 102577532; -.
DR   KEGG; sot:102577532; -.
DR   OrthoDB; 240595at2759; -.
DR   SABIO-RK; P32811; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P32811; baseline.
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; 1.
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; Carbohydrate metabolism; Cytoplasm;
KW   Direct protein sequencing; Glycosyltransferase; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..838
FT                   /note="Alpha-glucan phosphorylase, H isozyme"
FT                   /id="PRO_0000188542"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         684
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   838 AA;  95112 MW;  1F3A55BE0F0167B4 CRC64;
     MEGGAKSNDV SAAPIAQPLS EDPTDIASNI KYHAQYTPHF SPFKFEPLQA YYAATADSVR
     DRLIKQWNDT YLHYDKVNPK QTYYLSMEYL QGRALTNAVG NLDIHNAYAD ALNKLGQQLE
     EVVEQEKDAA LGNGGLGRLA SCFLDSMATL NLPAWGYGLR YRYGLFKQLI TKAGQEEVPE
     DWLEKFSPWE IVRHDVVFPI RFFGHVEVLP SGSRKWVGGE VLQALAYDVP IPGYRTKNTN
     SLRLWEAKAS SEDFNLFLFN DGQYDAAAQL HSRAQQICAV LYPGDATENG KLLRLKQQFF
     LCSASLQDII ARFKEREDGK GSHQWSEFPK KVAIQLNDTH PTLTIPELMR LLMDDEGLGW
     DESWNITTRT IAYTNHTVLP EALEKWSQAV MWKLLPRHME IIEEIDKRFV ATIMSERPDL
     ENKMPSMRIL DHNATKPVVH MANLCVVSSH TVNGVAQLHS DILKAELFAD YVSVWPTKFQ
     NKTNGITPRR WIRFCSPELS HIITKWLKTD QWVTNLELLA NLREFADNSE LHAEWESAKM
     ANKQRLAQYI LHVTGVSIDP NSLFDIQVKR IHEYKRQLLN ILGVIYRYKK LKGMSPEERK
     NTTPRTVMIG GKAFATYTNA KRIVKLVTDV GDVVNSDPDV NDYLKVVFVP NYNVSVAEML
     IPGSELSQHI STAGMEASGT SNMKFALNGC LIIGTLDGAN VEIREEIGED NFFLFGATAD
     EVPQLRKDRE NGLFKPDPRF EEAKQFIRSG AFGTYDYNPL LESLEGNSGY GRGDYFLVGH
     DFPSYMDAQA RVDEAYKDRK RWIKMSILST SGSGKFSSDR TISQYAKEIW NIAECRVP