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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001885602 – 797Maltodextrin phosphorylaseAdd BLAST796

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei251N6-acetyllysine1 Publication1
Modified residuei646N6-(pyridoxal phosphate)lysine1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP00490.
PaxDbiP00490.
PRIDEiP00490.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

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

Structurei

Secondary structure

1797
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 21Combined sources14
Helixi27 – 29Combined sources3
Helixi32 – 48Combined sources17
Beta strandi57 – 59Combined sources3
Beta strandi61 – 65Combined sources5
Helixi75 – 82Combined sources8
Helixi85 – 93Combined sources9
Turni94 – 96Combined sources3
Helixi99 – 103Combined sources5
Helixi115 – 129Combined sources15
Beta strandi134 – 139Combined sources6
Beta strandi147 – 151Combined sources5
Beta strandi154 – 158Combined sources5
Helixi164 – 166Combined sources3
Helixi174 – 176Combined sources3
Beta strandi178 – 183Combined sources6
Beta strandi188 – 190Combined sources3
Beta strandi195 – 208Combined sources14
Beta strandi210 – 212Combined sources3
Beta strandi215 – 224Combined sources10
Helixi231 – 235Combined sources5
Helixi241 – 243Combined sources3
Helixi244 – 250Combined sources7
Helixi251 – 253Combined sources3
Helixi263 – 290Combined sources28
Helixi295 – 297Combined sources3
Helixi298 – 301Combined sources4
Beta strandi302 – 309Combined sources8
Turni310 – 313Combined sources4
Helixi314 – 325Combined sources12
Helixi330 – 337Combined sources8
Turni338 – 340Combined sources3
Beta strandi341 – 344Combined sources4
Helixi350 – 352Combined sources3
Beta strandi355 – 357Combined sources3
Helixi358 – 364Combined sources7
Helixi366 – 386Combined sources21
Beta strandi387 – 389Combined sources3
Helixi391 – 397Combined sources7
Beta strandi399 – 401Combined sources3
Beta strandi404 – 406Combined sources3
Helixi407 – 414Combined sources8
Beta strandi415 – 422Combined sources8
Helixi423 – 431Combined sources9
Helixi435 – 440Combined sources6
Helixi442 – 444Combined sources3
Beta strandi445 – 447Combined sources3
Helixi454 – 457Combined sources4
Turni458 – 461Combined sources4
Helixi463 – 472Combined sources10
Beta strandi473 – 475Combined sources3
Helixi481 – 492Combined sources12
Helixi494 – 519Combined sources26
Beta strandi527 – 534Combined sources8
Helixi538 – 540Combined sources3
Helixi542 – 557Combined sources16
Beta strandi567 – 572Combined sources6
Helixi580 – 597Combined sources18
Turni600 – 602Combined sources3
Helixi603 – 605Combined sources3
Beta strandi606 – 610Combined sources5
Helixi616 – 622Combined sources7
Helixi623 – 625Combined sources3
Beta strandi627 – 631Combined sources5
Turni635 – 637Combined sources3
Helixi643 – 649Combined sources7
Beta strandi653 – 656Combined sources4
Helixi662 – 669Combined sources8
Helixi671 – 673Combined sources3
Beta strandi674 – 676Combined sources3
Helixi681 – 690Combined sources10
Helixi694 – 700Combined sources7
Helixi702 – 713Combined sources12
Turni714 – 719Combined sources6
Turni721 – 724Combined sources4
Helixi725 – 730Combined sources6
Turni733 – 735Combined sources3
Helixi741 – 760Combined sources20
Helixi762 – 775Combined sources14
Helixi777 – 779Combined sources3
Helixi781 – 791Combined sources11
Turni792 – 794Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OMAiEYCERIW.
PhylomeDBiP00490.

Family and domain databases

CDDicd04300. GT1_Glycogen_Phosphorylase. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti294K → E (PubMed:3037809).Curated1
Sequence conflicti294K → E (PubMed:3155826).Curated1
Sequence conflicti488E → V (PubMed:3037809).Curated1
Sequence conflicti488E → V (PubMed:3155826).Curated1
Sequence conflicti490F → L (PubMed:3037809).Curated1
Sequence conflicti490F → L (PubMed:3155826).Curated1
Sequence conflicti499Q → L (PubMed:3037809).Curated1
Sequence conflicti499Q → L (PubMed:3155826).Curated1
Sequence conflicti502E → V (PubMed:3037809).Curated1
Sequence conflicti502E → V (PubMed:3155826).Curated1
Sequence conflicti522E → D (PubMed:3037809).Curated1
Sequence conflicti522E → D (PubMed:3155826).Curated1
Sequence conflicti548H → R (PubMed:3155826).Curated1
Sequence conflicti682E → K (PubMed:3037809).Curated1
Sequence conflicti682E → K (PubMed:3155826).Curated1
Sequence conflicti688L → D (PubMed:3155826).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259324. 9 interactors.
DIPiDIP-10146N.
IntActiP00490. 26 interactors.
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.
OMAiEYCERIW.
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

CDDicd04300. GT1_Glycogen_Phosphorylase. 1 hit.
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...

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: November 2, 2016
This is version 157 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.