ID   PHSH_WHEAT              Reviewed;         832 AA.
AC   Q9LKJ3;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Alpha-glucan phosphorylase, H isozyme;
DE            EC=2.4.1.1;
DE   AltName: Full=Starch phosphorylase H;
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Star; TISSUE=Leaf;
RA   Schupp N.T., Ziegler P., Huebsch S.D.;
RT   "Full length clone of a cytosolic wheat leaf starch phosphorylase.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF275551; AAF82787.1; -; mRNA.
DR   AlphaFoldDB; Q9LKJ3; -.
DR   SMR; Q9LKJ3; -.
DR   STRING; 4565.Traes_3DL_FFCCD5827.1; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; Q9LKJ3; -.
DR   eggNOG; KOG2099; Eukaryota.
DR   BRENDA; 2.4.1.1; 6500.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q9LKJ3; baseline and differential.
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   2: Evidence at transcript level;
KW   Allosteric enzyme; Carbohydrate metabolism; Cytoplasm; Glycosyltransferase;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..832
FT                   /note="Alpha-glucan phosphorylase, H isozyme"
FT                   /id="PRO_0000188543"
FT   MOD_RES         678
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   832 AA;  93612 MW;  BEF45CA8EDCBB466 CRC64;
     MSAADKVKPA ASPASEDPSA IAGNISYHAQ YSPHFSPLAF GPEQAFYATA ESVRDHLLQR
     WNDTYLHFHK TDPKQTYYLS MEYLQGRALT NAVGNLAITG AYADALKKFG YELEAIAGQE
     RDAALGNGGL GRLASCFLDS MATLNLPSWG YGLRYRYGLF KQRIAKEGQE EIAEDWLDKF
     SPWEIVRHDV VYPIRFFGHV EISPDGKRKW AGGEVLNALA YDVPIPGYKT KNAISLRLWD
     ATATAEDFNL FQFNDGQYES AAQLHSRAQQ ICAVLYPGDA TEEGKLLRLK QQYFLCSASL
     QDIIFRFKER KADRVSGKWS EFPSKVAVQM NDTHPTLAIP ELMRLLMDVE GLGWDEAWAV
     TNKTVAYTNH TVLPEALEKW SQAVMKKLLP RHMEIIEEID KRFREMVIST RKDMEGKIES
     MRVLDNNPEK PVVRMANLCV VAGHTVNGVA ELHSNILKQE LFADYVSIWP NKFQNKTNGI
     TPRRWLRFCN PELSEIVTKW LKTDQWTSNL DLLTGLRKFA DDEKLHAEWA AAKLASKKRL
     AKHVLDVTGV TIDPDSLFDI QIKRIHEYKR QLMNILGAVY RYKKLKEMSA ADRQKVTPRT
     VMVGGKAFAT YTNAKRIVKL VNDVGAVVNN DADVNKYLKV VFIPNYNVSV AEVLIPGSEL
     SQHISTAGME ASGTSNMKFS LNGCVIIGTL DGANVEIREE VGQDNFFLFG AKADQVAGLR
     KDRENGLFKP DPRFEEAKQF IRSGAFGTYD YTPLLDSLEG NTGFGRGDYF LVGYDFPSYI
     DAQARVDEAY KDKKKWVKMS ILNTAGSGKF SSDRTIDQYA KEIWGISACP VP