A6WCK0 (A6WCK0_KINRD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Malto-oligosyltrehalose trehalohydrolase PIRNR PIRNR006337
Short name=MTHase PIRNR PIRNR006337
EC=3.2.1.141 PIRNR PIRNR006337

Alternative name(s):
4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase PIRNR PIRNR006337
Maltooligosyl trehalose trehalohydrolase PIRNR PIRNR006337

Gene names

Ordered Locus Names:

Krad_3075

Organism

Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216) [Complete proteome] [HAMAP] EMBL ABS04539.1

Taxonomic identifier

266940 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Kineosporiineae › Kineosporiaceae › Kineococcus

Protein attributes

Sequence length	583 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to yield trehalose and (1->4)-alpha-D-glucan. PIRNR PIRNR006337
Pathway	Glycan biosynthesis; trehalose biosynthesis. PIRNR PIRNR006337
Subcellular location	Cytoplasm By similarity PIRSR PIRSR006337-1.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family. PIRNR PIRNR006337

Ontologies

Keywords
Molecular function	Glycosidase PIRNR PIRNR006337 Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	trehalose biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4-alpha-D-{(1->4)-alpha-D-glucano}trehalose trehalohydrolase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	310 – 314	5	Substrate binding By similarity PIRSR PIRSR006337-2
Sites
	Active site	248	1	Nucleophile By similarity PIRSR PIRSR006337-1
	Active site	285	1	Proton donor By similarity PIRSR PIRSR006337-1
	Binding site	357	1	Substrate By similarity PIRSR PIRSR006337-2
	Site	381	1	Transition state stabilizer By similarity PIRSR PIRSR006337-3

Sequences

	Sequence		Length	Mass (Da)
	A6WCK0 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 5FDFC5B69A91157F	FASTA	583	63,156
	10 20 30 40 50 60 MLMEFGVWAP QAQQVDLVLD GEPVPMRRTG SPREGWWTAE AEGSHGTRYA FAVDGGDPRP 70 80 90 100 110 120 DPRSGWQPEG VHAASAVVDP STFSWTDGEW AGRDARGAVF YELHVGTFTP EGTFAAAAGK 130 140 150 160 170 180 LDHLVDLGVD VVEVLPVSAW DGPWNWGYDG VAPYAVQHEY GGPEGLAAFV DACHARGLAV 190 200 210 220 230 240 ALDCVYNHLG PSGNYLGEFG PYFTDKHDTP WGAAVNLDDA GSVEVRRWIV DNALRWFRDF 250 260 270 280 290 300 HVDALRLDAV HALVDDSEVH VLAQLADETA ALSRELGRPL SLVAESDLND AAMVTPTAEG 310 320 330 340 350 360 GRGMTAQWDD DVHHALHAWL TGERQGYYAD FGDAEVVKTT FEEAFFHAER FSTFRGEVWG 370 380 390 400 410 420 KRVDRSKVPG TAFLGYLQTH DQVGNRAVGD RIGHLLSPTA QAAGAALYLL GPFTPMVFMG 430 440 450 460 470 480 EEWNASTKWQ FFTSFPDPEL GKAVSTGRRS EFGQHGWDAE DVPDPQDPAT KDASVLRWEE 490 500 510 520 530 540 VSAPEHARVL DWYRTLTSLR RTVPAFADAD LREVRVDVAG NALVLHRGDH RVVVTLGGGA 550 560 570 580 DVDVEGAPVE VVAQFGDGPA AELLGEGVRT AGDAVVVVRV AGA

References

[1]

"Complete sequence of chromosome of Kineococcus radiotolerans SRS30216." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J., Fliermans C., Richardson P. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-149 / DSM 14245 / SRS30216.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000750 Genomic DNA. Translation: ABS04539.1.
RefSeq	YP_001362803.1. NC_009664.2.
3D structure databases
ProteinModelPortal	A6WCK0.
ModBase	Search...
Protein-protein interaction databases
STRING	A6WCK0.
Protein family/group databases
CAZy	CBM48. Carbohydrate-Binding Module Family 48. GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5336623.
GenomeReviews	Gene locus Krad_3075 in contig CP000750_GR.
KEGG	kra:Krad_3075.
NMPDR	fig|266940.1.peg.1429.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0296.
HOGENOM	HBG367595.
OMA	EGFVYQG.
ProtClustDB	CLSK2488256.
Family and domain databases
InterPro	IPR015902. Alpha_amylase. IPR006047. Glyco_hydro_13_cat_dom. IPR004193. Glyco_hydro_13_N. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR012768. Trehalose_TreZ. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
KO	K01236.
PANTHER	PTHR10357. Alpha_amylase. 1 hit. PTHR10357:SF21. PTHR10357:SF21. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02922. CBM_48. 1 hit. [Graphical view]
PIRSF	PIRSF006337. Trehalose_TreZ. 1 hit.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit. SSF81296. Ig_E-set. 1 hit.
TIGRFAMs	TIGR02402. Trehalose_TreZ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

A6WCK0_KINRD

Accession

Primary (citable) accession number: A6WCK0

Entry history

Integrated into UniProtKB/TrEMBL:	August 21, 2007
Last sequence update:	August 21, 2007
Last modified:	November 16, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)