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Reviewed, UniProtKB/Swiss-Prot O66937 (MALQ_AQUAE)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: malM
Ordered Locus Names: aq_723
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

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Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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 By similarity.

Sequence similarities

Belongs to the disproportionating enzyme family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4-alpha-glucanotransferase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4854854-alpha-glucanotransferase
PRO_0000170119

Secondary structure

1 .......................................................................................... 485
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O66937-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: D6D9B98BB90A0E22

FASTA48558,086
        10         20         30         40         50         60 
MRLAGILLHV TSLPSPYGIG DLGKEAYRFL DFLKECGFSL WQVLPLNPTS LEAGNSPYSS 

        70         80         90        100        110        120 
NSLFAGNYVL IDPEELLEED LIKERDLKRF PLGEALYEVV YEYKKELLEK AFKNFRRFEL 

       130        140        150        160        170        180 
LEDFLKEHSY WLRDYALYMA IKEEEGKEWY EWDEELKRRE KEALKRVLNK LKGRFYFHVF 

       190        200        210        220        230        240 
VQFVFFKQWE KLRRYARERG ISIVGDLPMY PSYSSADVWT NPELFKLDGD LKPLFVAGVP 

       250        260        270        280        290        300 
PDFFSKTGQL WGNPVYNWEE HEKEGFRWWI RRVHHNLKLF DFLRLDHFRG FEAYWEVPYG 

       310        320        330        340        350        360 
EETAVNGRWV KAPGKTLFKK LLSYFPKNPF IAEDLGFITD EVRYLRETFK IPGSRVIEFA 

       370        380        390        400        410        420 
FYDKESEHLP HNVEENNVYY TSTHDLPPIR GWFENLGEES RKRLFEYLGR EIKEEKVNEE 

       430        440        450        460        470        480 
LIRLVLISRA KFAIIQMQDL LNLGNEARMN YPGRPFGNWR WRIKEDYTQK KEFIKKLLGI 


YGREV

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References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

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Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC06897.1.
PIRE70363.
RefSeqNP_213497.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1TZ7X-ray2.15A/B1-485[»]
ModBaseSearch...

Protein family/group databases

CAZyGH77. Glycoside Hydrolase Family 77.

Genome annotation databases

GeneID1193386.
GenomeReviewsGene locus aq_723 in contig AE000657_GR.
KEGGaae:aq_723.
NMPDRfig|224324.1.peg.512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO66937.
OMAO66937. LQFAFDG.

Enzyme and pathway databases

BioCycAAEO224324:AQ_723-MON.
BRENDA2.4.1.25. 189781.

Family and domain databases

InterProIPR003385. Glyco_hydro_77.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF02446. Glyco_hydro_77. 1 hit.
[Graphical view]
TIGRFAMsTIGR00217. malQ. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameMALQ_AQUAE
AccessionPrimary (citable) accession number: O66937
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents