Maltooligosyltrehalose trehalohydrolase, putative - Deinococcus radiodurans

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Unreviewed, UniProtKB/TrEMBL Q9RX51 (Q9RX51_DEIRA)

Last modified June 16, 2009. Version 52. History...

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Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Submitted name:
Maltooligosyltrehalose trehalohydrolase, putative EMBL AAF10042.1

Gene names

Ordered Locus Names:

DR_0464

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	600 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	trehalose biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9RX51-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 594091EC093F8A44
Show »

600

66,910

        10         20         30         40         50         60 
MTQTQPVTPT PPASFQTQHD PRTRLGATPL PGGAGTRFRL WTSTARTVAV RVNGTEHVMT 

        70         80         90        100        110        120 
SLGGGIYELE LPVGPGARYL FVLDGVPTPD PYARFLPDGV HGEAEVVDFG TFDWTDADWH 

       130        140        150        160        170        180 
GIKLADCVFY EVHVGTFTPE GTYRAAAEKL PYLKELGVTA IQVMPLAAFD GQRGWGYDGA 

       190        200        210        220        230        240 
AFYAPYAPYG RPEDLMALVD AAHRLGLGVF LDVVYNHFGP SGNYLSSYAP SYFTDRFSSA 

       250        260        270        280        290        300 
WGMGLDYAEP HMRRYVTGNA RMWLRDYHFD GLRLDATPYM TDDSETHILT ELAQEIHELG 

       310        320        330        340        350        360 
GTHLLLAEDH RNLPDLVTVN HLDGIWTDDF HHETRVTLTG EQEGYYAGYR GGAEALAYTI 

       370        380        390        400        410        420 
RRGWRYEGQF WAVKGEEHER GHPSDALEAP NFVYCIQNHD QIGNRPLGER LHQSDGVTLH 

       430        440        450        460        470        480 
EYRGAAALLL PMTPLLFQGQ EWAASTPFQF FSDHAGELGQ AVSEGRKKEF GGFSGFSGED 

       490        500        510        520        530        540 
VPDPQAEQTF LNSKLNWAER EGGEHARTLR LYRDLLRLRR EDPVLHNRQR ENLTTGHDGD 

       550        560        570        580        590        600 
VLWVRTVTGA GERVLLWNLG QDTRAVAEVK LPFTVPRRLL LHTEGREDLT LGAGEAVLVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.
[2]	"Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides." Timmins J., Leiros H.K., Leonard G., Leiros I., McSweeney S. J. Mol. Biol. 347:949-963(2005) [PubMed: 15784255] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

AE000513 Genomic DNA. Translation: AAF10042.1.

PIR

RefSeq

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BHU	X-ray	1.10	A	1-600	[»]
2BHY	X-ray	1.50	A	1-600	[»]
2BHZ	X-ray	1.20	A	1-600	[»]
2BXY	X-ray	1.75	A	1-600	[»]
2BXZ	X-ray	1.75	A	1-600	[»]
2BY0	X-ray	1.55	A	1-600	[»]
2BY1	X-ray	1.55	A	1-600	[»]
2BY2	X-ray	1.50	A	1-600	[»]
2BY3	X-ray	1.50	A	1-600	[»]

ModBase

Protein family/group databases

CAZy

CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Genome annotation databases

GeneID

GenomeReviews

Gene locus DR_0464 in contig AE000513_GR.

KEGG

NMPDR

fig|243230.1.peg.646.

TIGR

Phylogenomic databases

HOGENOM

OMA

Q9RX51. EAVIYEL.

Enzyme and pathway databases

BioCyc

DRAD243230:DR_0464-MON.

Family and domain databases

InterPro

IPR006047. Glyco_hydro_13_cat.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_sg_catalytic.
IPR013783. Ig-like_fold.
IPR012768. Trehalose_TreZ.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]

PIRSF

PIRSF006337. Trehalose_TreZ. 1 hit.

TIGRFAMs

TIGR02402. trehalose_TreZ. 1 hit.

ProtoNet

Entry information

Entry name

Q9RX51_DEIRA

Accession

Primary (citable) accession number: Q9RX51

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information