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P80099 (MGTA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:mgtA
Ordered Locus Names:TM_0364
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandCalcium
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4-alpha-glucanotransferase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4414414-alpha-glucanotransferase
PRO_0000054336

Sites

Active site1861Nucleophile
Active site2161Proton donor
Metal binding131Calcium
Metal binding151Calcium
Metal binding171Calcium
Metal binding191Calcium; via carbonyl oxygen
Metal binding211Calcium
Site2781Transition state stabilizer By similarity

Experimental info

Sequence conflict11M → A AA sequence Ref.2

Secondary structure

1 ................................................................................. 441
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80099 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 9FB4C2ABC9D3DF3A

FASTA44151,843
        10         20         30         40         50         60 
MIGYQIYVRS FRDGNLDGVG DFRGLKNAVS YLKELGIDFV WLMPVFSSIS FHGYDVVDFY 

        70         80         90        100        110        120 
SFKAEYGSER EFKEMIEAFH DSGIKVVLDL PIHHTGFLHT WFQKALKGDP HYRDYYVWAN 

       130        140        150        160        170        180 
KETDLDERRE WDGEKIWHPL EDGRFYRGLF GPFSPDLNYD NPQVFDEMKR LVLHLLDMGV 

       190        200        210        220        230        240 
DGFRFDAAKH MRDTIEQNVR FWKYFLSDLK GIFLAEIWAE ARMVDEHGRI FGYMLNFDTS 

       250        260        270        280        290        300 
HCIKEAVWKE NTRVLIESIE RAVIGKDYLP VNFTSNHDMS RLASFEGGFS KEKIKLSISI 

       310        320        330        340        350        360 
LFTLPGVPLV FYGDELGMKG VYQKPNTEVV LDPFPWNESM CVEGQTFWKW PAYNGPFSGI 

       370        380        390        400        410        420 
SVEYQKRDPD SILSHTLGWT RFRKENQWID RAKLEFLCKE DKFLVYRLYD DQHSLKVFHN 

       430        440 
LSGEEVVFEG VKMKPYKTEV V

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Purification and characterization of a novel thermostable 4-alpha-glucanotransferase of Thermotoga maritima cloned in Escherichia coli."
Liebl W., Feil R., Gabelsberger J., Kellermann J., Schleifer K.-H.
Eur. J. Biochem. 207:81-88(1992) [PubMed: 1628664] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-23, CHARACTERIZATION.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and its acarbose complex: implications for substrate specificity and catalysis."
Roujeinikova A., Raasch C., Sedelnikova S., Liebl W., Rice D.W.
J. Mol. Biol. 321:149-162(2002) [PubMed: 12139940] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000512 Genomic DNA. Translation: AAD35451.1.
RefSeqNP_228175.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LWHX-ray2.60A/B1-441[»]
1LWJX-ray2.50A/B1-441[»]
ProteinModelPortalP80099.
SMRP80099. Positions 1-441.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID897323.
GenomeReviewsGene locus TM_0364 in contig AE000512_GR.
KEGGtma:TM0364.
NMPDRfig|243274.1.peg.359.
PATRIC23935609. VBITheMar51294_0369.
TIGRTM_0364.

Phylogenomic databases

HOGENOMHBG669028.
OMALDERREW.
PhylomeDBP80099.
ProtClustDBCLSK875110.

Enzyme and pathway databases

BioCycTMAR243274:TM_0364-MONOMER.

Family and domain databases

InterProIPR015261. 4-alpha-glucanotransf_C.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.
KOK00705.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF09178. DUF1945. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMGTA_THEMA
AccessionPrimary (citable) accession number: P80099
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 30, 2000
Last modified: January 25, 2012
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

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