Q32H58 (OTSA_SHIDS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming]
EC=2.4.1.15

Alternative name(s):
Osmoregulatory trehalose synthesis protein A
Trehalose-6-phosphate synthase
UDP-glucose-glucosephosphate glucosyltransferase

Gene names

Name:	otsA
Ordered Locus Names:	SDY_1193

Organism

Shigella dysenteriae serotype 1 (strain Sd197) [Reference proteome] [HAMAP]

Taxonomic identifier

300267 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella › Shigella dysenteriae

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of glucose from UDP-glucose to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor By similarity.
Catalytic activity	UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.
Pathway	Glycan biosynthesis; trehalose biosynthesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the glycosyltransferase 20 family.

Ontologies

Keywords
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	trehalose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 474	474	Alpha,alpha-trehalose-phosphate synthase [UDP-forming]		PRO_0000348919
Regions
	Region	22 – 23	2	UDP-glucose binding By similarity
	Region	366 – 370	5	UDP-glucose binding By similarity
Sites
	Binding site	10	1	Glucose-6-phosphate By similarity
	Binding site	77	1	Glucose-6-phosphate By similarity
	Binding site	131	1	Glucose-6-phosphate By similarity
	Binding site	263	1	UDP-glucose By similarity
	Binding site	268	1	UDP-glucose By similarity
	Binding site	301	1	Glucose-6-phosphate By similarity
	Binding site	340	1	UDP-glucose; via amide nitrogen and carbonyl oxygen By similarity
	Site	86	1	Involved in alpha anomer selectivity By similarity
	Site	156	1	Involved in alpha anomer selectivity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q32H58 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 63FFB6F938056F95	FASTA	474	53,611
	10 20 30 40 50 60 MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN 70 80 90 100 110 120 ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL 130 140 150 160 170 180 LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCDY 190 200 210 220 230 240 DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP 250 260 270 280 290 300 LPPKLAQLKA ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS 310 320 330 340 350 360 RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL 370 380 390 400 410 420 RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS 430 440 450 460 470 LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA

References

[1]

"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery." Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q. Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sd197.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000034 Genomic DNA. Translation: ABB61347.1.
RefSeq	YP_402838.1. NC_007606.1.
3D structure databases
ProteinModelPortal	Q32H58.
SMR	Q32H58. Positions 2-458.
ModBase	Search...
Protein-protein interaction databases
STRING	300267.SDY_1193.
Protein family/group databases
CAZy	GT20. Glycosyltransferase Family 20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABB61347; ABB61347; SDY_1193.
GeneID	3795494.
KEGG	sdy:SDY_1193.
PATRIC	18691905. VBIShiDys99784_1412.
Phylogenomic databases
eggNOG	COG0380.
HOGENOM	HOG000191478.
KO	K00697.
OMA	EYGRKEM.
ProtClustDB	PRK10117.
Enzyme and pathway databases
BioCyc	SDYS300267:GJEW-1189-MONOMER.
UniPathway	UPA00299.
Family and domain databases
InterPro	IPR001830. Glyco_trans_20. IPR012766. Trehalose_OtsA. [Graphical view]
Pfam	PF00982. Glyco_transf_20. 1 hit. [Graphical view]
TIGRFAMs	TIGR02400. trehalose_OtsA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

OTSA_SHIDS

Accession

Primary (citable) accession number: Q32H58

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	December 6, 2005
Last modified:	May 29, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program