PHSM_KLEPN
ID PHSM_KLEPN Reviewed; 108 AA.
AC P07094;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Maltodextrin phosphorylase;
DE EC=2.4.1.1;
DE Flags: Fragment;
GN Name=malP;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2946664; DOI=10.1128/jb.168.3.1220-1227.1986;
RA Bloch M.-A., Raibaud O.;
RT "Comparison of the malA regions of Escherichia coli and Klebsiella
RT pneumoniae.";
RL J. Bacteriol. 168:1220-1227(1986).
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; M14735; AAA25086.1; -; Genomic_DNA.
DR AlphaFoldDB; P07094; -.
DR SMR; P07094; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PRIDE; P07094; -.
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:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000811; Glyco_trans_35.
DR PANTHER; PTHR11468; PTHR11468; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Carbohydrate metabolism; Glycosyltransferase;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..>108
FT /note="Maltodextrin phosphorylase"
FT /id="PRO_0000188561"
FT NON_TER 108
SQ SEQUENCE 108 AA; 12325 MW; 3D624CFB6F5D4F1B CRC64;
MSQTSFNKAQ FQAALTRQWQ HFGLQSASEM TQRQWWRAVS GALSELLSAQ PVAKATEGER
HVNYISMEFL IGRLTGNNLL NLGWYQQVSD ELQAHDVNLT DLLEEEID