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P80099

- MGTA_THEMA

UniProt

P80099 - MGTA_THEMA

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Protein

4-alpha-glucanotransferase

Gene

mgtA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.

Cofactori

Binds 1 calcium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131Calcium
Metal bindingi15 – 151Calcium
Metal bindingi17 – 171Calcium
Metal bindingi19 – 191Calcium; via carbonyl oxygen
Metal bindingi21 – 211Calcium
Active sitei186 – 1861Nucleophile
Active sitei216 – 2161Proton donor
Sitei278 – 2781Transition state stabilizerBy similarity

GO - Molecular functioni

  1. 4-alpha-glucanotransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
4-alpha-glucanotransferase (EC:2.4.1.25)
Alternative name(s):
Amylomaltase
Disproportionating enzyme
Short name:
D-enzyme
Gene namesi
Name:mgtA
Ordered Locus Names:TM_0364
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4414414-alpha-glucanotransferasePRO_0000054336Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi243274.TM0364.

Structurei

Secondary structure

1
441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64
Helixi8 – 114
Beta strandi14 – 196
Helixi22 – 276
Helixi29 – 346
Beta strandi39 – 424
Beta strandi49 – 524
Beta strandi57 – 626
Turni64 – 663
Helixi69 – 8113
Beta strandi85 – 906
Helixi100 – 1067
Helixi110 – 1134
Beta strandi130 – 1323
Beta strandi137 – 1393
Beta strandi145 – 1473
Beta strandi159 – 1613
Helixi162 – 17615
Turni177 – 1793
Beta strandi182 – 1854
Helixi188 – 1903
Beta strandi191 – 1944
Helixi195 – 20511
Turni206 – 2083
Beta strandi211 – 2155
Helixi221 – 23111
Beta strandi232 – 2354
Helixi237 – 24812
Helixi253 – 26210
Beta strandi267 – 2748
Helixi282 – 2843
Turni285 – 2873
Helixi291 – 30212
Beta strandi304 – 3118
Turni312 – 3176
Helixi327 – 3304
Beta strandi336 – 3405
Beta strandi356 – 3594
Helixi362 – 3654
Helixi372 – 38514
Helixi387 – 3893
Beta strandi393 – 3997
Beta strandi401 – 41010
Beta strandi413 – 4208
Beta strandi422 – 4243
Beta strandi426 – 4283
Beta strandi431 – 4333
Beta strandi438 – 4403

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LWHX-ray2.60A/B1-441[»]
1LWJX-ray2.50A/B1-441[»]
ProteinModelPortaliP80099.
SMRiP80099. Positions 1-441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80099.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Phylogenomic databases

eggNOGiCOG0366.
InParanoidiP80099.
KOiK00705.
OMAiLDERREW.
OrthoDBiEOG6RZB0T.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR015261. 4-alpha-glucanotransf_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09178. DUF1945. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

P80099-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIGYQIYVRS FRDGNLDGVG DFRGLKNAVS YLKELGIDFV WLMPVFSSIS
60 70 80 90 100
FHGYDVVDFY SFKAEYGSER EFKEMIEAFH DSGIKVVLDL PIHHTGFLHT
110 120 130 140 150
WFQKALKGDP HYRDYYVWAN KETDLDERRE WDGEKIWHPL EDGRFYRGLF
160 170 180 190 200
GPFSPDLNYD NPQVFDEMKR LVLHLLDMGV DGFRFDAAKH MRDTIEQNVR
210 220 230 240 250
FWKYFLSDLK GIFLAEIWAE ARMVDEHGRI FGYMLNFDTS HCIKEAVWKE
260 270 280 290 300
NTRVLIESIE RAVIGKDYLP VNFTSNHDMS RLASFEGGFS KEKIKLSISI
310 320 330 340 350
LFTLPGVPLV FYGDELGMKG VYQKPNTEVV LDPFPWNESM CVEGQTFWKW
360 370 380 390 400
PAYNGPFSGI SVEYQKRDPD SILSHTLGWT RFRKENQWID RAKLEFLCKE
410 420 430 440
DKFLVYRLYD DQHSLKVFHN LSGEEVVFEG VKMKPYKTEV V
Length:441
Mass (Da):51,843
Last modified:May 30, 2000 - v2
Checksum:i9FB4C2ABC9D3DF3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → A AA sequence (PubMed:1628664)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35451.1.
RefSeqiNP_228175.1. NC_000853.1.
YP_007976712.1. NC_021214.1.
YP_008990663.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35451; AAD35451; TM_0364.
GeneIDi18092434.
897323.
KEGGitma:TM0364.
tmi:THEMA_02895.
tmm:Tmari_0362.
PATRICi23935609. VBITheMar51294_0369.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35451.1 .
RefSeqi NP_228175.1. NC_000853.1.
YP_007976712.1. NC_021214.1.
YP_008990663.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LWH X-ray 2.60 A/B 1-441 [» ]
1LWJ X-ray 2.50 A/B 1-441 [» ]
ProteinModelPortali P80099.
SMRi P80099. Positions 1-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM0364.

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

DNASUi 897323.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35451 ; AAD35451 ; TM_0364 .
GeneIDi 18092434.
897323.
KEGGi tma:TM0364.
tmi:THEMA_02895.
tmm:Tmari_0362.
PATRICi 23935609. VBITheMar51294_0369.

Phylogenomic databases

eggNOGi COG0366.
InParanoidi P80099.
KOi K00705.
OMAi LDERREW.
OrthoDBi EOG6RZB0T.

Miscellaneous databases

EvolutionaryTracei P80099.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR015261. 4-alpha-glucanotransf_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF09178. DUF1945. 1 hit.
[Graphical view ]
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiMGTA_THEMA
AccessioniPrimary (citable) accession number: P80099
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3