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   02-SEP-2026, entry version 81.
DE   RecName: Full=Maltodextrin phosphorylase;
DE            EC=2.4.1.1;
DE   Flags: Fragment;
GN   Name=malP;
OS   Klebsiella pneumoniae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Klebsiella;
OC   Klebsiella pneumoniae complex.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M14735; AAA25086.1; -; Genomic_DNA.
DR   AlphaFoldDB; P07094; -.
DR   SMR; P07094; -.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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
//