B2GJ34 (B2GJ34_KOCRD) 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

Name:	treZ EMBL BAG29004.1
Ordered Locus Names:	KRH_06570

Organism

Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201) [Complete proteome] [HAMAP]

Taxonomic identifier

378753 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Kocuria

Protein attributes

Sequence length	606 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 EMBL BAG29004.1 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
Sites
	Active site	264	1	Nucleophile By similarity PIRSR PIRSR006337-1
	Active site	301	1	Proton donor By similarity PIRSR PIRSR006337-1
	Site	397	1	Transition state stabilizer By similarity PIRSR PIRSR006337-3

Sequences

	Sequence		Length	Mass (Da)
	B2GJ34 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 6A0AD11765EB5B76	FASTA	606	67,890
	10 20 30 40 50 60 MSTDHRFDVW APHARKVTVR IEGEDHPMEG LDGRPGWWTL PADDAAPQGT VRYGYILTKT 70 80 90 100 110 120 FDEGTPEERE QVSDVLPDPR SRRQPQGVHD LSCTFDADAF EWHDADFRPR PLQDSVLYEL 130 140 150 160 170 180 HPGTFTPVGT LDAAIGRLDH LVDLGVTAVE LLPVNGFNGE HNWGYDGVAW YTVAEPYGGP 190 200 210 220 230 240 EAYQRFVDAC HARGLSVIQD VVYNHLGPSG NYLPLFADYF KPGASSWGDL INLDGWGADG 250 260 270 280 290 300 VREYILDNVT MWLREYHVDG FRLDAVHALA DSSAKHILEE IAERVAEEVQ RTGKDLVTIA 310 320 330 340 350 360 ESDLNDPRMI AATHRHGLGM GAQWLDDVHH AAHTAFTGET QGYYGDFASL HALEKTMHTA 370 380 390 400 410 420 YFHNGTYSTF RGRSHGREID PVEQRPYQFV TFLQNHDQVG NRAAGDRMNQ SMSVDRAIAA 430 440 450 460 470 480 ATWLMAQPFT PMLFMGEEYG ASTPWQFFTA HPEPELGEAV AKGRKAEFAQ MAWDHATVPD 490 500 510 520 530 540 PQDPQTFERS KLNWAEVHEG DHERIYRAYR DLIALRRNTP ELTDQRWDTV ATQASDSEQW 550 560 570 580 590 600 FVLKRMTEPE SEHGVVIAIN LGREPRNLPL MGGDAPRLLF TSGTGPEPGA EGTVRVAPET AVVLRV

References

[1]

"Complete genome sequence of the soil actinomycete Kocuria rhizophila." Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S. J. Bacteriol. 190:4139-4146(2008) [PubMed: 18408034] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP009152 Genomic DNA. Translation: BAG29004.1.
RefSeq	YP_001854510.1. NC_010617.1.
3D structure databases
ProteinModelPortal	B2GJ34.
ModBase	Search...
Protein-protein interaction databases
STRING	B2GJ34.
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	6239953.
GenomeReviews	Gene locus KRH_06570 in contig AP009152_GR.
KEGG	krh:KRH_06570.
PATRIC	22181548. VBIKocRhi5258_0645.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG367595.
OMA	EGFVYQG.
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. IPR022567. Maltooligo_trehalose_bac_C. 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. 2 hits. PF02922. CBM_48. 1 hit. PF11941. DUF3459. 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

B2GJ34_KOCRD

Accession

Primary (citable) accession number: B2GJ34

Entry history

Integrated into UniProtKB/TrEMBL:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	December 14, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)