Skip Header

Contribute Send feedback
Read comments (?) or add your own

P00490 (PHSM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Maltodextrin phosphorylase
EC=2.4.1.1
Gene names
Name:malP
Ordered Locus Names:b3417, JW5689
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length797 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

(1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the glycogen phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 797796Maltodextrin phosphorylase
PRO_0000188560

Amino acid modifications

Modified residue2511N6-acetyllysine Ref.10
Modified residue6461N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict2941K → E Ref.1
Sequence conflict2941K → E Ref.5
Sequence conflict4881E → V Ref.1
Sequence conflict4881E → V Ref.5
Sequence conflict4901F → L Ref.1
Sequence conflict4901F → L Ref.5
Sequence conflict4991Q → L Ref.1
Sequence conflict4991Q → L Ref.5
Sequence conflict5021E → V Ref.1
Sequence conflict5021E → V Ref.5
Sequence conflict5221E → D Ref.1
Sequence conflict5221E → D Ref.5
Sequence conflict5481H → R Ref.5
Sequence conflict6821E → K Ref.1
Sequence conflict6821E → K Ref.5
Sequence conflict6881L → D Ref.5

Secondary structure

1 ............................................................................................................................................. 797
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00490 [UniParc].

Last modified January 23, 2007. Version 7.
Checksum: 61E450AAF75C896A

FASTA79790,522
        10         20         30         40         50         60 
MSQPIFNDKQ FQEALSRQWQ RYGLNSAAEM TPRQWWLAVS EALAEMLRAQ PFAKPVANQR 

        70         80         90        100        110        120 
HVNYISMEFL IGRLTGNNLL NLGWYQDVQD SLKAYDINLT DLLEEEIDPA LGNGGLGRLA 

       130        140        150        160        170        180 
ACFLDSMATV GQSATGYGLN YQYGLFRQSF VDGKQVEAPD DWHRSNYPWF RHNEALDVQV 

       190        200        210        220        230        240 
GIGGKVTKDG RWEPEFTITG QAWDLPVVGY RNGVAQPLRL WQATHAHPFD LTKFNDGDFL 

       250        260        270        280        290        300 
RAEQQGINAE KLTKVLYPND NHTAGKKLRL MQQYFQCACS VADILRRHHL AGRKLHELAD 

       310        320        330        340        350        360 
YEVIQLNDTH PTIAIPELLR VLIDEHQMSW DDAWAITSKT FAYTNHTLMP EALERWDVKL 

       370        380        390        400        410        420 
VKGLLPRHMQ IINEINTRFK TLVEKTWPGD EKVWAKLAVV HDKQVHMANL CVVGGFAVNG 

       430        440        450        460        470        480 
VAALHSDLVV KDLFPEYHQL WPNKFHNVTN GITPRRWIKQ CNPALAALLD KSLQKEWAND 

       490        500        510        520        530        540 
LDQLINLEKF ADDAKFRQQY REIKQANKVR LAEFVKVRTG IEINPQAIFD IQIKRLHEYK 

       550        560        570        580        590        600 
RQHLNLLHIL ALYKEIRENP QADRVPRVFL FGAKAAPGYY LAKNIIFAIN KVADVINNDP 

       610        620        630        640        650        660 
LVGDKLKVVF LPDYCVSAAE KLIPAADISE QISTAGKEAS GTGNMKLALN GALTVGTLDG 

       670        680        690        700        710        720 
ANVEIAEKVG EENIFIFGHT VEQVKAILAK GYDPVKWRKK DKVLDAVLKE LESGKYSDGD 

       730        740        750        760        770        780 
KHAFDQMLHS IGKQGGDPYL VMADFAAYVE AQKQVDVLYR DQEAWTRAAI LNTARCGMFS 

       790 
SDRSIRDYQA RIWQAKR

« Hide

References

« Hide 'large scale' references
[1]"E. coli maltodextrin phosphorylase: primary structure and deletion mapping of the C-terminal site."
Palm D., Goerl R., Weidinger G., Zeier R., Fischer B., Schinzel R.
Z. Naturforsch. C 42:394-400(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 701.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Evolution of catalytic and regulatory sites in phosphorylases."
Palm D., Goerl R., Burger K.J.
Nature 313:500-502(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-688.
[6]"Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase."
Pugsley A.P., Dubreuil C.
Mol. Microbiol. 2:473-479(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-797.
[7]"A DNA sequence containing the control sites for gene malT and for the malPQ operon."
Debarbouille M., Cossart P., Raibaud O.
Mol. Gen. Genet. 185:88-92(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
[8]"Use of deletions created in vitro to map transcriptional regulatory signals in the malA region of Escherichia coli."
Raibaud O., Debarbouille M., Schwartz M.
J. Mol. Biol. 163:395-408(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
[9]"N-terminal sequences of Escherichia coli and potato phosphorylase."
Schiltz E., Palm D., Klein H.W.
FEBS Lett. 109:59-62(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20.
[10]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-251, MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[11]"The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase."
Watson K.A., Schinzel R., Palm D., Johnson L.N.
EMBO J. 16:1-14(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[12]"The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex."
O'Reilly M., Watson K.A., Johnson L.N.
Biochemistry 38:5337-5345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS).
[13]"Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question."
Watson K.A., McCleverty C., Geremia S., Cottaz S., Driguez H., Johnson L.N.
EMBO J. 18:4619-4632(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X06791 Genomic DNA. Translation: CAA29949.1.
U18997 Genomic DNA. Translation: AAA58215.1. Sequence problems.
U00096 Genomic DNA. Translation: AAT48180.1.
AP009048 Genomic DNA. Translation: BAE77874.1.
X02003 Genomic DNA. Translation: CAA26035.1.
M32793 Genomic DNA. Translation: AAA24105.1.
M24342 Genomic DNA. Translation: AAA24108.1.
V00304 Genomic DNA. Translation: CAA23584.1.
PIRPHECGM. D65137.
RefSeqYP_026218.1. NC_000913.2.
YP_492015.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHPX-ray3.00A/B2-795[»]
1E4OX-ray2.90A/B2-796[»]
1L5VX-ray2.00A/B2-797[»]
1L5WX-ray1.80A/B2-797[»]
1L6IX-ray2.20A/B2-797[»]
1QM5X-ray2.00A/B2-797[»]
2ASVX-ray1.95A/B2-796[»]
2AV6X-ray2.01A/B2-796[»]
2AW3X-ray2.20A/B2-796[»]
2AZDX-ray2.16A/B2-796[»]
2ECPX-ray2.95A/B2-795[»]
ProteinModelPortalP00490.
SMRP00490. Positions 2-797.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10146N.
IntActP00490. 26 interactions.
MINTMINT-1225428.
STRING511145.b3417.

Protein family/group databases

CAZyGT35. Glycosyltransferase Family 35.

Proteomic databases

PaxDbP00490.
PRIDEP00490.

Protocols and materials databases

DNASU947922.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48180; AAT48180; b3417.
BAE77874; BAE77874; BAE77874.
GeneID12930330.
947922.
KEGGecj:Y75_p3759.
eco:b3417.
PATRIC32122272. VBIEscCol129921_3513.

Organism-specific databases

EchoBASEEB0555.
EcoGeneEG10560. malP.

Phylogenomic databases

eggNOGCOG0058.
HOGENOMHOG000278445.
KOK00688.
OMATESFDFY.
ProtClustDBPRK14985.

Enzyme and pathway databases

BioCycEcoCyc:MALDEXPHOSPHORYL-MONOMER.
ECOL316407:JW5689-MONOMER.
MetaCyc:MALDEXPHOSPHORYL-MONOMER.
SABIO-RKP00490.

Gene expression databases

GenevestigatorP00490.

Family and domain databases

InterProIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERPTHR11468. PTHR11468. 1 hit.
PfamPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsTIGR02093. P_ylase. 1 hit.
PROSITEPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00490.

Entry information

Entry namePHSM_ECOLI
AccessionPrimary (citable) accession number: P00490
Secondary accession number(s): Q2M782, Q9R783
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 133 of the entry and version 7 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents