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Alpha-glucan phosphorylase, H isozyme (EC 2.4.1.1) (Starch phosphorylase H)

 PHSH_VICFA              Reviewed;         842 AA.
P53537;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 69.
RecName: Full=Alpha-glucan phosphorylase, H isozyme;
EC=2.4.1.1;
AltName: Full=Starch phosphorylase H;
Vicia faba (Broad bean) (Faba vulgaris).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Fabeae; Vicia.
NCBI_TaxID=3906;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Fribo; TISSUE=Cotyledon;
PubMed=8680306; DOI=10.1007/BF00196882;
Buchner P., Borisjuk L., Wobus U.;
"Glucan phosphorylases in Vicia faba L.: cloning, structural analysis
and expression patterns of cytosolic and plastidic forms in relation
to starch.";
Planta 199:64-73(1996).
-!- FUNCTION: Phosphorylase is an important allosteric enzyme in
carbohydrate metabolism. Enzymes from different sources differ in
their regulatory mechanisms and in their natural substrates.
However, all known phosphorylases share catalytic and structural
properties.
-!- FUNCTION: The H isoform exhibits higher affinity for branched
polyglucans such as soluble starch or glycogen.
-!- CATALYTIC ACTIVITY: ((1->4)-alpha-D-glucosyl)(n) + phosphate =
((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the glycogen phosphorylase family.
{ECO:0000305}.
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EMBL; Z35117; CAA84494.1; -; mRNA.
PIR; T12091; T12091.
ProteinModelPortal; P53537; -.
SMR; P53537; -.
CAZy; GT35; Glycosyltransferase Family 35.
PRIDE; P53537; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
CDD; cd04300; GT1_Glycogen_Phosphorylase; 1.
InterPro; IPR011833; Glycg_phsphrylas.
InterPro; IPR000811; Glyco_trans_35.
InterPro; IPR035090; Pyridoxal_P_attach_site.
PANTHER; PTHR11468; PTHR11468; 1.
Pfam; PF00343; Phosphorylase; 1.
PIRSF; PIRSF000460; Pprylas_GlgP; 1.
TIGRFAMs; TIGR02093; P_ylase; 1.
PROSITE; PS00102; PHOSPHORYLASE; 1.
2: Evidence at transcript level;
Allosteric enzyme; Carbohydrate metabolism; Cytoplasm;
Glycosyltransferase; Pyridoxal phosphate; Transferase.
CHAIN 1 842 Alpha-glucan phosphorylase, H isozyme.
/FTId=PRO_0000188544.
MOD_RES 688 688 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
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


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