B2HQ83 (B2HQ83_MYCMM) 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 ACC40826.1
Ordered Locus Names:	MMAR_2377

Organism

Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]

Taxonomic identifier

216594 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	587 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	381	1	Transition state stabilizer By similarity PIRSR PIRSR006337-3

Sequences

	Sequence		Length	Mass (Da)
	B2HQ83 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 33E70025A1EA19FE	FASTA	587	64,408
	10 20 30 40 50 60 MTEFRVWAPK PELVRLDVEG GVYPMRRTDD GWWHTAIETA PAARYGFLLD DDPKVLPDPR 70 80 90 100 110 120 SARQPDGVHA RSQLWNPAAA TWTDGAWTGR SVTGAVIYEL HVGTFTAAGT FDSAIEKLDY 130 140 150 160 170 180 LVDLGIDFVE LMPVNSFAGT HGWGYDGVLW YSVHEPYGGP AGLVRFVDAC HARGLGVLID 190 200 210 220 230 240 AVFNHLGPSG NYLPRFGPYL SSASNPWGEG INIADADSDE VRRYIIGAAL RWMREFHADG 250 260 270 280 290 300 LRLDAVHALV DTTAVPILEE LATETDWLSK QVGRPLSLVA ESDLNDPRLI TPRDGGGYGI 310 320 330 340 350 360 TAQWDDDIHH AIHTAVSGER QGYYADFGAN SDSMATLAHT LRRGFFHAGT YSSFRRRRHG 370 380 390 400 410 420 RPLDTATIPA TRLLAYTCTH DQVGNRALGD RPSQNLTSGQ LAIKAALVLG SPYTAMLFMG 430 440 450 460 470 480 EEWGASSPFQ FFSSHPEPEL AVATAQGRKA EFAEHGWDAD EIPDPQDPQT FLRSKLVWGE 490 500 510 520 530 540 GDSGEHAQLL RFYRDLIALR HHETDLADPW LDHLVIDYDE QQSWIIMRRG RFGIACNLGT 550 560 570 580 EATTVPLSGA LVLGWGEPNT SDSGTELAGH SVAVLRCDQS TAPAEPA

References

[1]

"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T. Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000854 Genomic DNA. Translation: ACC40826.1.
RefSeq	YP_001850681.1. NC_010612.1.
3D structure databases
ProteinModelPortal	B2HQ83.
ModBase	Search...
Protein-protein interaction databases
STRING	B2HQ83.
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
EnsemblBacteria	EBMYCT00000033451; EBMYCP00000031891; EBMYCG00000033446.
GeneID	6226641.
GenomeReviews	Gene locus MMAR_2377 in contig CP000854_GR.
KEGG	mmi:MMAR_2377.
PATRIC	18065703. VBIMycMar75906_2533.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016657.
HOGENOM	HBG367595.
OMA	EGFVYQG.
ProtClustDB	CLSK799816.
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. 1 hit. 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

B2HQ83_MYCMM

Accession

Primary (citable) accession number: B2HQ83

Entry history

Integrated into UniProtKB/TrEMBL:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	December 14, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)