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A5CQX1 (A5CQX1_CLAM3) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 CAN01475.1
Ordered Locus Names:CMM_1430
OrganismClavibacter michiganensis subsp. michiganensis (strain NCPPB 382) [Complete proteome] [HAMAP] EMBL CAN01475.1
Taxonomic identifier443906 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length600 AA.
Sequence statusComplete.
Protein existenceInferred 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site2521Nucleophile By similarity PIRSR PIRSR006337-1
Active site2891Proton donor By similarity PIRSR PIRSR006337-1
Site3851Transition state stabilizer By similarity PIRSR PIRSR006337-3

Sequences

Sequence LengthMass (Da)Tools
A5CQX1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 6C47BF54381F2BF3

FASTA60065,853
        10         20         30         40         50         60 
MTDDRFDIWA PKARTLALSV GDERLPLSPV GDGWWTLDAD RAEALPSGDL DYGYLVDDAE 

        70         80         90        100        110        120 
TPLPDPRSRR QPEGVHGRSR TYDPSSFAWT DQAWTGRQLA GAVIYEMHIG TFTPDGTLDS 

       130        140        150        160        170        180 
AIDRLDHLVA LGVDLVEVLP VNGFNGTHNW GYDGVLWYTV QETYGGPEAY QRFVDACHAR 

       190        200        210        220        230        240 
GLGVVQDVVY NHLGPSGNYL PVYGPYLHEA SANTWGSSLN LDGEDSGPVR EYIIDNALMW 

       250        260        270        280        290        300 
LGDYHVDALR LDAVHALVDD TATHLLEELA VQVDVLSAHV GRPLTLIAES DLNDPKLITS 

       310        320        330        340        350        360 
REAHGYGLDA QWSDDFHHAV HVALTGETTG YYEDFASLGA LAKVITRGFF HDGTWSSFRG 

       370        380        390        400        410        420 
RVHGRPLDTE RIPAHRLVVA NQNHDQIGNR ATGDRLTATL DEGGLALAAV LTLTSPFTPM 

       430        440        450        460        470        480 
LFMGEEWGAT TSWQFFTSHP EHDLGEATAK GRIAEFAKMG WDESVVPNPQ DLSTFQDSKL 

       490        500        510        520        530        540 
DWSELYGTEA AESQHARLFS LYSELIRLRR AHPDLTDPRF AEVEVEVHEE ARLLVMDRGE 

       550        560        570        580        590        600 
LSIVVNLSDE ERRVPVVGER PALLLATAPG VALGDDEVVL PARSAAILGP VADSAEALLA 

« Hide

References

[1]"The genome sequence of the tomato-pathogenic actinomycete Clavibacter michiganensis subsp. michiganensis NCPPB382 reveals a large island involved in pathogenicity."
Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M., Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O., Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C. expand/collapse author list , Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O., Bartels D.
J. Bacteriol. 190:2138-2149(2008) [PubMed: 18192381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM711867 Genomic DNA. Translation: CAN01475.1.
RefSeqYP_001222171.1. NC_009480.1.

3D structure databases

ProteinModelPortalA5CQX1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5CQX1.

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5172960.
GenomeReviewsGene locus CMM_1430 in contig AM711867_GR.
KEGGcmi:CMM_1430.
PATRIC21453633. VBIClaMic82482_1540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0296.
HOGENOMHBG367595.
OMAEGFVYQG.
ProtClustDBCLSK2320911.

Family and domain databases

InterProIPR015902. 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]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
KOK01236.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PTHR10357:SF21. PTHR10357:SF21. 1 hit.
PfamPF00128. Alpha-amylase. 2 hits.
PF11941. DUF3459. 1 hit.
[Graphical view]
PIRSFPIRSF006337. Trehalose_TreZ. 1 hit.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
TIGRFAMsTIGR02402. Trehalose_TreZ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA5CQX1_CLAM3
AccessionPrimary (citable) accession number: A5CQX1
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)