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A1TFL3 (OTSA_MYCVP) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Trehalose-phosphate synthase

Short name=TPS
EC=2.4.1.-
Alternative name(s):
Trehalose-6-phosphate synthase
Gene names
Name:otsA
Ordered Locus Names:Mvan_5192
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of glucose from a nucleoside diphosphate-glucose to glucose-6-phosphate to form trehalose-6-phosphate and nucleoside diphosphate By similarity.

Catalytic activity

Nucleoside diphosphate-glucose + D-glucose 6-phosphate = trehalose 6-phosphate + nucleoside diphosphate.

Pathway

Glycan biosynthesis; trehalose biosynthesis.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the glycosyltransferase 20 family.

Ontologies

Keywords
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtrehalose biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular functiontransferase activity, transferring glycosyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Trehalose-phosphate synthase
PRO_0000348925

Regions

Region42 – 432NDP-glucose binding By similarity
Region399 – 4035NDP-glucose binding By similarity

Sites

Binding site221Glucose-6-phosphate By similarity
Binding site1001Glucose-6-phosphate By similarity
Binding site1541Glucose-6-phosphate By similarity
Binding site2961NDP-glucose By similarity
Binding site3011NDP-glucose By similarity
Binding site3341Glucose-6-phosphate By similarity
Site1091Involved in alpha anomer selectivity By similarity
Site1791Involved in alpha anomer selectivity By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TFL3 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 2F76B7B78E911B3F

FASTA49155,034
        10         20         30         40         50         60 
MAPQSGPEAR SGGADFVVVA NRLPIDMVRR ADGTTEFKRS PGGLVTALEP LLRRRHGAWI 

        70         80         90        100        110        120 
GWPGVPEDAD DPNAATEPIE QDGMTLVPVR LSSEDVAEYY EGFSNATLWP LYHDVIVKPI 

       130        140        150        160        170        180 
YHREWWDRYV DVNRRFAEAT AHTAAEGATV WVQDYQLQLV PKMLRMLRPD LTIGFFLHIP 

       190        200        210        220        230        240 
FPPVELFMQM PWRTEIIEGL LGADLVGFHL PGGAQNFLIL ARRLIGATTS RGNVGVRSRF 

       250        260        270        280        290        300 
GEVQFGFRTV KVGAFPISID SAELDQHARS RATRQRAKEI RAELGNPRKI LLGVDRLDYT 

       310        320        330        340        350        360 
KGIDVRLRAF SELLEEGRID PEDTVLVQLA TPSRERVESY VAMREDIERQ VGHVNGEFGE 

       370        380        390        400        410        420 
VGHPVLHYLH RPIPREDLVA FFVAADVMLV TPLRDGMNLV AKEYVACRHD LGGALVLSEF 

       430        440        450        460        470        480 
TGAAAELRQA YLTNPHHIEG VKDAIEAALT QAPEEGRRRM RAMRRQVLAH DVDRWARSFL 

       490 
DALASKEPVE G 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM15963.1.
RefSeqYP_955969.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1TFL3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TFL3.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000077525; EBMYCP00000075478; EBMYCG00000077520.
GeneID4645709.
GenomeReviewsGene locus Mvan_5192 in contig CP000511_GR.
KEGGmva:Mvan_5192.
PATRIC18188795. VBIMycVan31953_5292.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0380.
GeneTreeEBGT00050000016525.
HOGENOMHBG559076.
OMAEYGRKEM.
PhylomeDBA1TFL3.
ProtClustDBCLSK872185.

Enzyme and pathway databases

BioCycMVAN350058:MVAN_5192-MONOMER.

Family and domain databases

InterProIPR001830. Glyco_trans_20.
[Graphical view]
KOK00697.
PfamPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOTSA_MYCVP
AccessionPrimary (citable) accession number: A1TFL3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families