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A1UM30 (OTSA_MYCSK) 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:Mkms_4697
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP]
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length489 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 – 489489Trehalose-phosphate synthase
PRO_0000348912

Regions

Region42 – 432NDP-glucose binding By similarity
Region393 – 3975NDP-glucose binding By similarity

Sites

Binding site221Glucose-6-phosphate By similarity
Binding site941Glucose-6-phosphate By similarity
Binding site1481Glucose-6-phosphate By similarity
Binding site2901NDP-glucose By similarity
Binding site2951NDP-glucose By similarity
Binding site3281Glucose-6-phosphate By similarity
Site1031Involved in alpha anomer selectivity By similarity
Site1731Involved in alpha anomer selectivity By similarity

Sequences

Sequence LengthMass (Da)Tools
A1UM30 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: D8C558B2C21386D8

FASTA48954,726
        10         20         30         40         50         60 
MASEGDPGVG SGDSDFVVVA NRLPIDMERL PDGSTSFKRS PGGLVTALEP LLRKRHGAWI 

        70         80         90        100        110        120 
GWAGIPDSAE DPIEDDGLQL YPVSLSADDV ADYYEGFSNA TLWPLYHDLI VKPIYHRKWW 

       130        140        150        160        170        180 
DRYVEVNRRF AEATARAAAE GATVWVQDYQ LQLVPKMLRM LRPDLTIGFF LHIPFPPVEL 

       190        200        210        220        230        240 
FMQMPWRTEI IEGLLGADLV GFHLPGGAQN FLYLARRLTG ANTSRATVGV RSRFGEVQVG 

       250        260        270        280        290        300 
FRTVKVGAFP ISIDSDELDG KARNRAVRQR AREIRNELGN PRKILLGVDR LDYTKGINVR 

       310        320        330        340        350        360 
LEALSELLED GRVDSHDTVF VQLATPSRER VQSYIEMRED IERQVGHING EFGDVGHPIV 

       370        380        390        400        410        420 
HYLHRPIPRD ELIAFFVAAD VMLVTPLRDG MNLVAKEYVA CRSDLGGALV LSEFTGAAAE 

       430        440        450        460        470        480 
LRQAYLANPH HLEGVKDAIE AALNQDPEEG RRRMRALRRQ VLAHDVDRWA RAFLDALADT 


RAGAKPVRD

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000518 Genomic DNA. Translation: ABL93888.1.
RefSeqYP_940678.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1UM30.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1UM30.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000056182; EBMYCP00000054406; EBMYCG00000056177.
GeneID4616112.
GenomeReviewsGene locus Mkms_4697 in contig CP000518_GR.
KEGGmkm:Mkms_4697.
PATRIC18108442. VBIMycSp70743_5229.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0380.
GeneTreeEBGT00050000016525.
HOGENOMHBG559076.
OMAEYGRKEM.
ProtClustDBCLSK872185.

Enzyme and pathway databases

BioCycMSP189918:MKMS_4697-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_MYCSK
AccessionPrimary (citable) accession number: A1UM30
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

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