Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Maltodextrin phosphorylase

Gene

malP

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

GO - Molecular functioni

  • glycogen phosphorylase activity Source: GO_Central
  • maltodextrin phosphorylase activity Source: EcoliWiki
  • pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  • alpha-glucan catabolic process Source: EcoliWiki
  • glycogen catabolic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:MALDEXPHOSPHORYL-MONOMER.
ECOL316407:JW5689-MONOMER.
MetaCyc:MALDEXPHOSPHORYL-MONOMER.
BRENDAi2.4.1.1. 2026.
SABIO-RKP00490.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Names & Taxonomyi

Protein namesi
Recommended name:
Maltodextrin phosphorylase (EC:2.4.1.1)
Gene namesi
Name:malP
Ordered Locus Names:b3417, JW5689
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10560. malP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 797796Maltodextrin phosphorylasePRO_0000188560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei251 – 2511N6-acetyllysine1 Publication
Modified residuei646 – 6461N6-(pyridoxal phosphate)lysine

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP00490.
PaxDbiP00490.
PRIDEiP00490.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4259324. 9 interactions.
DIPiDIP-10146N.
IntActiP00490. 26 interactions.
MINTiMINT-1225428.
STRINGi511145.b3417.

Structurei

Secondary structure

1
797
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2114Combined sources
Helixi27 – 293Combined sources
Helixi32 – 4817Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 655Combined sources
Helixi75 – 828Combined sources
Helixi85 – 939Combined sources
Turni94 – 963Combined sources
Helixi99 – 1035Combined sources
Helixi115 – 12915Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi154 – 1585Combined sources
Helixi164 – 1663Combined sources
Helixi174 – 1763Combined sources
Beta strandi178 – 1836Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi195 – 20814Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi215 – 22410Combined sources
Helixi231 – 2355Combined sources
Helixi241 – 2433Combined sources
Helixi244 – 2507Combined sources
Helixi251 – 2533Combined sources
Helixi263 – 29028Combined sources
Helixi295 – 2973Combined sources
Helixi298 – 3014Combined sources
Beta strandi302 – 3098Combined sources
Turni310 – 3134Combined sources
Helixi314 – 32512Combined sources
Helixi330 – 3378Combined sources
Turni338 – 3403Combined sources
Beta strandi341 – 3444Combined sources
Helixi350 – 3523Combined sources
Beta strandi355 – 3573Combined sources
Helixi358 – 3647Combined sources
Helixi366 – 38621Combined sources
Beta strandi387 – 3893Combined sources
Helixi391 – 3977Combined sources
Beta strandi399 – 4013Combined sources
Beta strandi404 – 4063Combined sources
Helixi407 – 4148Combined sources
Beta strandi415 – 4228Combined sources
Helixi423 – 4319Combined sources
Helixi435 – 4406Combined sources
Helixi442 – 4443Combined sources
Beta strandi445 – 4473Combined sources
Helixi454 – 4574Combined sources
Turni458 – 4614Combined sources
Helixi463 – 47210Combined sources
Beta strandi473 – 4753Combined sources
Helixi481 – 49212Combined sources
Helixi494 – 51926Combined sources
Beta strandi527 – 5348Combined sources
Helixi538 – 5403Combined sources
Helixi542 – 55716Combined sources
Beta strandi567 – 5726Combined sources
Helixi580 – 59718Combined sources
Turni600 – 6023Combined sources
Helixi603 – 6053Combined sources
Beta strandi606 – 6105Combined sources
Helixi616 – 6227Combined sources
Helixi623 – 6253Combined sources
Beta strandi627 – 6315Combined sources
Turni635 – 6373Combined sources
Helixi643 – 6497Combined sources
Beta strandi653 – 6564Combined sources
Helixi662 – 6698Combined sources
Helixi671 – 6733Combined sources
Beta strandi674 – 6763Combined sources
Helixi681 – 69010Combined sources
Helixi694 – 7007Combined sources
Helixi702 – 71312Combined sources
Turni714 – 7196Combined sources
Turni721 – 7244Combined sources
Helixi725 – 7306Combined sources
Turni733 – 7353Combined sources
Helixi741 – 76020Combined sources
Helixi762 – 77514Combined sources
Helixi777 – 7793Combined sources
Helixi781 – 79111Combined sources
Turni792 – 7943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHPX-ray3.00A/B1-795[»]
1E4OX-ray2.90A/B2-797[»]
1L5VX-ray2.00A/B2-797[»]
1L5WX-ray1.80A/B2-797[»]
1L6IX-ray2.20A/B2-797[»]
1QM5X-ray2.00A/B2-797[»]
2ASVX-ray1.95A/B2-797[»]
2AV6X-ray2.01A/B2-797[»]
2AW3X-ray2.20A/B2-797[»]
2AZDX-ray2.16A/B2-797[»]
2ECPX-ray2.95A/B2-795[»]
ProteinModelPortaliP00490.
SMRiP00490. Positions 2-797.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00490.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycogen phosphorylase family.Curated

Phylogenomic databases

eggNOGiENOG4107QQN. Bacteria.
COG0058. LUCA.
HOGENOMiHOG000278445.
InParanoidiP00490.
KOiK00688.
OMAiHAINNVA.
OrthoDBiEOG60SCHC.
PhylomeDBiP00490.

Family and domain databases

InterProiIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERiPTHR11468. PTHR11468. 1 hit.
PfamiPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsiTIGR02093. P_ylase. 1 hit.
PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00490-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPIFNDKQ FQEALSRQWQ RYGLNSAAEM TPRQWWLAVS EALAEMLRAQ
60 70 80 90 100
PFAKPVANQR HVNYISMEFL IGRLTGNNLL NLGWYQDVQD SLKAYDINLT
110 120 130 140 150
DLLEEEIDPA LGNGGLGRLA ACFLDSMATV GQSATGYGLN YQYGLFRQSF
160 170 180 190 200
VDGKQVEAPD DWHRSNYPWF RHNEALDVQV GIGGKVTKDG RWEPEFTITG
210 220 230 240 250
QAWDLPVVGY RNGVAQPLRL WQATHAHPFD LTKFNDGDFL RAEQQGINAE
260 270 280 290 300
KLTKVLYPND NHTAGKKLRL MQQYFQCACS VADILRRHHL AGRKLHELAD
310 320 330 340 350
YEVIQLNDTH PTIAIPELLR VLIDEHQMSW DDAWAITSKT FAYTNHTLMP
360 370 380 390 400
EALERWDVKL VKGLLPRHMQ IINEINTRFK TLVEKTWPGD EKVWAKLAVV
410 420 430 440 450
HDKQVHMANL CVVGGFAVNG VAALHSDLVV KDLFPEYHQL WPNKFHNVTN
460 470 480 490 500
GITPRRWIKQ CNPALAALLD KSLQKEWAND LDQLINLEKF ADDAKFRQQY
510 520 530 540 550
REIKQANKVR LAEFVKVRTG IEINPQAIFD IQIKRLHEYK RQHLNLLHIL
560 570 580 590 600
ALYKEIRENP QADRVPRVFL FGAKAAPGYY LAKNIIFAIN KVADVINNDP
610 620 630 640 650
LVGDKLKVVF LPDYCVSAAE KLIPAADISE QISTAGKEAS GTGNMKLALN
660 670 680 690 700
GALTVGTLDG ANVEIAEKVG EENIFIFGHT VEQVKAILAK GYDPVKWRKK
710 720 730 740 750
DKVLDAVLKE LESGKYSDGD KHAFDQMLHS IGKQGGDPYL VMADFAAYVE
760 770 780 790
AQKQVDVLYR DQEAWTRAAI LNTARCGMFS SDRSIRDYQA RIWQAKR
Length:797
Mass (Da):90,522
Last modified:January 23, 2007 - v7
Checksum:i61E450AAF75C896A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941K → E (PubMed:3037809).Curated
Sequence conflicti294 – 2941K → E (PubMed:3155826).Curated
Sequence conflicti488 – 4881E → V (PubMed:3037809).Curated
Sequence conflicti488 – 4881E → V (PubMed:3155826).Curated
Sequence conflicti490 – 4901F → L (PubMed:3037809).Curated
Sequence conflicti490 – 4901F → L (PubMed:3155826).Curated
Sequence conflicti499 – 4991Q → L (PubMed:3037809).Curated
Sequence conflicti499 – 4991Q → L (PubMed:3155826).Curated
Sequence conflicti502 – 5021E → V (PubMed:3037809).Curated
Sequence conflicti502 – 5021E → V (PubMed:3155826).Curated
Sequence conflicti522 – 5221E → D (PubMed:3037809).Curated
Sequence conflicti522 – 5221E → D (PubMed:3155826).Curated
Sequence conflicti548 – 5481H → R (PubMed:3155826).Curated
Sequence conflicti682 – 6821E → K (PubMed:3037809).Curated
Sequence conflicti682 – 6821E → K (PubMed:3155826).Curated
Sequence conflicti688 – 6881L → D (PubMed:3155826).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD65137. PHECGM.
RefSeqiWP_000081909.1. NZ_LN832404.1.
YP_026218.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48180; AAT48180; b3417.
BAE77874; BAE77874; BAE77874.
GeneIDi947922.
KEGGiecj:JW5689.
eco:b3417.
PATRICi32122272. VBIEscCol129921_3513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD65137. PHECGM.
RefSeqiWP_000081909.1. NZ_LN832404.1.
YP_026218.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHPX-ray3.00A/B1-795[»]
1E4OX-ray2.90A/B2-797[»]
1L5VX-ray2.00A/B2-797[»]
1L5WX-ray1.80A/B2-797[»]
1L6IX-ray2.20A/B2-797[»]
1QM5X-ray2.00A/B2-797[»]
2ASVX-ray1.95A/B2-797[»]
2AV6X-ray2.01A/B2-797[»]
2AW3X-ray2.20A/B2-797[»]
2AZDX-ray2.16A/B2-797[»]
2ECPX-ray2.95A/B2-795[»]
ProteinModelPortaliP00490.
SMRiP00490. Positions 2-797.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259324. 9 interactions.
DIPiDIP-10146N.
IntActiP00490. 26 interactions.
MINTiMINT-1225428.
STRINGi511145.b3417.

Protein family/group databases

CAZyiGT35. Glycosyltransferase Family 35.

Proteomic databases

EPDiP00490.
PaxDbiP00490.
PRIDEiP00490.

Protocols and materials databases

DNASUi947922.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48180; AAT48180; b3417.
BAE77874; BAE77874; BAE77874.
GeneIDi947922.
KEGGiecj:JW5689.
eco:b3417.
PATRICi32122272. VBIEscCol129921_3513.

Organism-specific databases

EchoBASEiEB0555.
EcoGeneiEG10560. malP.

Phylogenomic databases

eggNOGiENOG4107QQN. Bacteria.
COG0058. LUCA.
HOGENOMiHOG000278445.
InParanoidiP00490.
KOiK00688.
OMAiHAINNVA.
OrthoDBiEOG60SCHC.
PhylomeDBiP00490.

Enzyme and pathway databases

BioCyciEcoCyc:MALDEXPHOSPHORYL-MONOMER.
ECOL316407:JW5689-MONOMER.
MetaCyc:MALDEXPHOSPHORYL-MONOMER.
BRENDAi2.4.1.1. 2026.
SABIO-RKP00490.

Miscellaneous databases

EvolutionaryTraceiP00490.
PROiP00490.

Family and domain databases

InterProiIPR011833. Glycg_phsphrylas.
IPR000811. Glyco_trans_35.
[Graphical view]
PANTHERiPTHR11468. PTHR11468. 1 hit.
PfamiPF00343. Phosphorylase. 1 hit.
[Graphical view]
PIRSFiPIRSF000460. Pprylas_GlgP. 1 hit.
TIGRFAMsiTIGR02093. P_ylase. 1 hit.
PROSITEiPS00102. PHOSPHORYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. 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, IDENTIFICATION BY 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).

Entry informationi

Entry nameiPHSM_ECOLI
AccessioniPrimary (citable) accession number: P00490
Secondary accession number(s): Q2M782, Q9R783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 154 of the entry and version 7 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.