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P15977 (MALQ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-alpha-glucanotransferase
EC=2.4.1.25
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name=D-enzyme
Gene names
Name:malQ
Synonyms:malA
Ordered Locus Names:b3416, JW3379
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length694 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Transfers a segment of a (1->4)-alpha-D-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-D-glucan.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the disproportionating enzyme family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmaltose catabolic process

Inferred from mutant phenotype PubMed 4891257. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-alpha-glucanotransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6946944-alpha-glucanotransferase
PRO_0000170125

Experimental info

Sequence conflict221A → P in AAA24106. Ref.1
Sequence conflict199 – 2002SP → TA in AAA24106. Ref.1
Sequence conflict380 – 3812AE → GT in AAA24106. Ref.1
Sequence conflict4621G → R in AAA24106. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15977 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 73FFB3F8E5619311

FASTA69478,503
        10         20         30         40         50         60 
MESKRLDNAA LAAGISPNYI NAHGKPQSIS AETKRRLLDA MHQRTATKVA VTPVPNVMVY 

        70         80         90        100        110        120 
TSGKKMPMVV EGSGEYSWLL TTEEGTQYKG HVTGGKAFNL PTKLPEGYHT LTLTQDDQRA 

       130        140        150        160        170        180 
HCRVIVAPKR CYEPQALLNK QKLWGACVQL YTLRSEKNWG IGDFGDLKAM LVDVAKRGGS 

       190        200        210        220        230        240 
FIGLNPIHAL YPANPESASP YSPSSRRWLN VIYIDVNAVE DFHLSEEAQA WWQLPTTQQT 

       250        260        270        280        290        300 
LQQARDADWV DYSTVTALKM TALRMAWKGF AQRDDEQMAA FRQFVAEQGD SLFWQAAFDA 

       310        320        330        340        350        360 
LHAQQVKEDE MRWGWPAWPE MYQNVDSPEV RQFCEEHRDD VDFYLWLQWL AYSQFAACWE 

       370        380        390        400        410        420 
ISQGYEMPIG LYRDLAVGVA EGGAETWCDR ELYCLKASVG APPDILGPLG QNWGLPPMDP 

       430        440        450        460        470        480 
HIITARAYEP FIELLRANMQ NCGALRIDHV MSMLRLWWIP YGETADQGAY VHYPVDDLLS 

       490        500        510        520        530        540 
ILALESKRHR CMVIGEDLGT VPVEIVGKLR SSGVYSYKVL YFENDHEKTF RAPKAYPEQS 

       550        560        570        580        590        600 
MAVAATHDLP TLRGYWECGD LTLGKTLGLY PDEVVLRGLY QDRELAKQGL LDALHKYGCL 

       610        620        630        640        650        660 
PKRAGHKASL MSMTPTLNRG LQRYIADSNS ALLGLQPEDW LDMAEPVNIP GTSYQYKNWR 

       670        680        690 
RKLSATLESM FADDGVNKLL KDLDRRRRAA AKKK

« Hide

References

« Hide 'large scale' references
[1]"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].
[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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M32793 Genomic DNA. Translation: AAA24106.1.
U18997 Genomic DNA. Translation: AAA58214.1.
U00096 Genomic DNA. Translation: AAC76441.1.
AP009048 Genomic DNA. Translation: BAE77875.1.
PIRC65137.
RefSeqNP_417875.1. NC_000913.2.
YP_492016.1. NC_007779.1.

3D structure databases

ProteinModelPortalP15977.
SMRP15977. Positions 250-556.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10147N.
IntActP15977. 6 interactions.
MINTMINT-1275716.
STRING511145.b3416.

Protein family/group databases

CAZyGH77. Glycoside Hydrolase Family 77.

Proteomic databases

PaxDbP15977.
PRIDEP15977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76441; AAC76441; b3416.
BAE77875; BAE77875; BAE77875.
GeneID12932222.
947923.
KEGGecj:Y75_p3760.
eco:b3416.
PATRIC32122270. VBIEscCol129921_3512.

Organism-specific databases

EchoBASEEB0556.
EcoGeneEG10561. malQ.

Phylogenomic databases

eggNOGCOG1640.
HOGENOMHOG000245168.
KOK00705.
OMAFYLYLQF.
ProtClustDBPRK11052.

Enzyme and pathway databases

BioCycEcoCyc:AMYLOMALT-MONOMER.
ECOL316407:JW3379-MONOMER.
MetaCyc:AMYLOMALT-MONOMER.

Gene expression databases

GenevestigatorP15977.

Family and domain databases

Gene3D3.20.20.80. 2 hits.
InterProIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
TIGRFAMsTIGR00217. malQ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMALQ_ECOLI
AccessionPrimary (citable) accession number: P15977
Secondary accession number(s): Q2M781
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 111 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

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