Q82L53 (Q82L53_STRAW) 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:	amyA2 EMBL BAC69870.1
Ordered Locus Names:	SAV_2159 EMBL BAC69870.1

Organism

Streptomyces avermitilis [Complete proteome] [HAMAP]

Taxonomic identifier

33903 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	581 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
Sites
	Active site	244	1	Nucleophile By similarity PIRSR PIRSR006337-1
	Active site	281	1	Proton donor By similarity PIRSR PIRSR006337-1
	Site	379	1	Transition state stabilizer By similarity PIRSR PIRSR006337-3

Sequences

	Sequence		Length	Mass (Da)
	Q82L53 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: C3E24AE4229F1299	FASTA	581	63,692
	10 20 30 40 50 60 MQFEVWAPQA ARVTLHCGGA TRALARDEER DGWWKGDAEA GDGTRYGFAL DDGAVLPDPR 70 80 90 100 110 120 SRRQPDGPDG LSAVVDHGRY AWRADRPGRG LPGAVLYELH VGTYTREGTL DAAAERLGHL 130 140 150 160 170 180 VELGVTHVEL MPLCPFPGRH GWGYEGVSLW AVHEPYGGPE ALKRFVDRAH ELGLGVVLDV 190 200 210 220 230 240 VHNHLGPSGN CLPAFGPYFT DTHHTPWGAA VNLDAPGSDE VRAYLVGSAL AWLRDYRVDG 250 260 270 280 290 300 LRLDAVHALC DTRACHFLEE LSTAVDALAA DQDRPLFLVA ESDLNDPRLV TPRHEGGLGL 310 320 330 340 350 360 HAQWNDDFHH ALHTALTGES QGYYEDFARA PFAALAKTLT GGFFHDGTYS TFRGRCHGRP 370 380 390 400 410 420 LDRTRVSAHR LLGYAQTHDQ VGNRAQGDRL SASLSPGLLA CAATLTLTSA FTPMLFMGEE 430 440 450 460 470 480 WAAGTPWQFF TDHTDPELAE AVRRGRRREF AAHGWAEEDV PDPQDPATRD RSCLDWAEPE 490 500 510 520 530 540 SGIHARVLAW YRGLITLRHH EADLSDPDLT DVKVAYDEEA RWIAFRRGDV RVAVNLSKEP 550 560 570 580 ARIPLGLAHA RVLAAWEPVE TPGADGVLEL PGESSVVLTQ A

References

[1]

"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000030 Genomic DNA. Translation: BAC69870.1.
RefSeq	NP_823335.1. NC_003155.4.
3D structure databases
HSSP	HSSP built from PDB template 1EH9 based on UniProtKB Q55088.
ProteinModelPortal	Q82L53.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1210358.
GenomeReviews	Gene locus SAV2159 in contig BA000030_GR.
KEGG	sma:SAV_2159.
NMPDR	fig|227882.1.peg.2161.
PATRIC	23717787. VBIStrAve112782_2311.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG367595.
OMA	EGFVYQG.
ProtClustDB	CLSK375663.
Enzyme and pathway databases
BioCyc	SAVE227882:SAV2159-MONOMER.
Family and domain databases
InterPro	IPR015902. Alpha_amylase. IPR006047. Glyco_hydro_13_cat_dom. 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. 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

Q82L53_STRAW

Accession

Primary (citable) accession number: Q82L53

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)