ID   PHSH_VICFA              Reviewed;         842 AA.
AC   P53537;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Alpha-glucan phosphorylase, H isozyme;
DE            EC=2.4.1.1;
DE   AltName: Full=Starch phosphorylase H;
OS   Vicia faba (Broad bean) (Faba vulgaris).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Fribo; TISSUE=Cotyledon;
RX   PubMed=8680306; DOI=10.1007/bf00196882;
RA   Buchner P., Borisjuk L., Wobus U.;
RT   "Glucan phosphorylases in Vicia faba L.: cloning, structural analysis and
RT   expression patterns of cytosolic and plastidic forms in relation to
RT   starch.";
RL   Planta 199:64-73(1996).
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   -!- FUNCTION: The H isoform exhibits higher affinity for branched
CC       polyglucans such as soluble starch or glycogen.
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; Z35117; CAA84494.1; -; mRNA.
DR   PIR; T12091; T12091.
DR   AlphaFoldDB; P53537; -.
DR   SMR; P53537; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   GO; GO:0005737; C:cytoplasm; 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; 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; Transferase.
FT   CHAIN           1..842
FT                   /note="Alpha-glucan phosphorylase, H isozyme"
FT                   /id="PRO_0000188544"
FT   MOD_RES         688
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   842 AA;  95924 MW;  6EA0C09069DC63B4 CRC64;
     MGFKVETNGG DGSLVSAKVP PLANPLAEKP DEIASNISYH AQYTPHFSPF KFQLQQAYYA
     TAESVRDRLI QQWNETYLHF HKVDPKQTYY LSMEFLQGRA LTNAIGNLNI QDAYADALRK
     FGLELEEITE QEKDAALGNG GLGRLASCFL DSMATLNLPA WGYGLRYRYG LFKQIITKEG
     QEEVAEDWLE KFSPWEIVRH DVLYPIRFFG QVEVNPDGSR QWIGGEVIQA LAYDVPIPGY
     QTKNTISLRL WEAKACADDF DLFLFNDGQL ESASVLHSRA QQICSVLYPG DATEGGKLLR
     LKQQYFLCSA SLQDIISRFK ERRQGPWNWS EFPTKVAVQL NDTHPTLSIP ELMRLLMDDE
     GLGWDEAWAV TSKTVAYTNH TVLPEALEKW SQPVMWKLLP RHMEIIEEID RRFVALISKT
     RLDLEDEVSN MRILDNNLQK PVVRMANLCV VSSHTVNGVA QLHSDILKSE LFASYVSIWP
     TKFQNKTNGI TPRRWINFCS PELSRIITKW LKTDKWVTNL DLLTGLREFA DNEDLQAEWL
     SAKRANKQRL AQYVLQVTGE NIDPDSLFDI QVKRIHEYKR QLLNILGVIY RYKKLKEMSP
     EERKSTTART VMIGGKAFAT YTNAKRIVKL VDDVGSVVNS DPEVNSYLKV VFVPNYNVSV
     AEVLIPGSEL SQHISTAGME ASGTSNMKFA LNRVLIIGTL DGANVEIREE IGEENFFLFG
     ATADEVPRLR KERENGLFKP DPRFEEAKKF IRSGVFGSYD YNPLLDSLEG NSGYGRGDYF
     LVGYDFPSYM DAQEKVDEAY RDKKRWLKMS ILSTAGSGKF SSDRTIAQYA KEIWNIEECR
     VP