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Protein

Alpha-amylase

Gene

amy

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Enzyme and pathway databases

BioCyciXCAM190485:GIXZ-747-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
Gene namesi
Name:amyImported
Ordered Locus Names:XCC0748Imported
OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)Imported
Taxonomic identifieri190485 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001010 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi190485.XCC0748.

Structurei

3D structure databases

ProteinModelPortaliQ7CLU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Phylogenomic databases

KOiK01176.
OMAiNYHINAV.
OrthoDBiEOG6K6V4W.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7CLU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHATSRPCPR TFWQRAHQLL LIALTLLLTT ASAQADVILH AFNWPYATVE
60 70 80 90 100
ARAKQIADAG YRKVLVAPAY RSEGSAWWAR YQPQDIRLID NPLGDTTAFA
110 120 130 140 150
RMVQALANNG VETYADVVFN HMANEAATRS DLNYPGSAVL AQYAANPGRY
160 170 180 190 200
DALRLFGTVQ SNFLSASDFG PAQCISNYND AFQVRNYRIC GGGSDPGLPD
210 220 230 240 250
LLGNDWVVQQ QRAYLQALKG LGVTGFRVDA AKHMTFDHLN RVFDAGIRSG
260 270 280 290 300
VYVFGEVITG GGSGNGDYDQ FLAPYLQSTP HAAYDFPLFN AVRNAFGVGA
310 320 330 340 350
SMQQLVDPAS TGQALPGNRA VTFAVTHDIP NNAGFRYAIL DPVDETLAYA
360 370 380 390 400
YLLGRNGGVP MVYTDNNESG DNRWVNAYLR DDLRRMIGFH NGVQGSDMQV
410 420 430 440 450
LSSSACHILF RRGSLGIVGI NKCGNPVNTT VAMNGSVLFW NADYVDALGS
460 470
GTVVRISSGS YTFTLPARQA RMWRR
Length:475
Mass (Da):51,839
Last modified:July 5, 2004 - v1
Checksum:i981AC0D90777488C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008922 Genomic DNA. Translation: AAM40063.1.
RefSeqiNP_636139.1. NC_003902.1.
WP_011035984.1. NC_003902.1.

Genome annotation databases

EnsemblBacteriaiAAM40063; AAM40063; XCC0748.
GeneIDi1001375.
KEGGixcc:XCC0748.
PATRICi24072156. VBIXanCam115730_0813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008922 Genomic DNA. Translation: AAM40063.1.
RefSeqiNP_636139.1. NC_003902.1.
WP_011035984.1. NC_003902.1.

3D structure databases

ProteinModelPortaliQ7CLU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190485.XCC0748.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM40063; AAM40063; XCC0748.
GeneIDi1001375.
KEGGixcc:XCC0748.
PATRICi24072156. VBIXanCam115730_0813.

Phylogenomic databases

KOiK01176.
OMAiNYHINAV.
OrthoDBiEOG6K6V4W.

Enzyme and pathway databases

BioCyciXCAM190485:GIXZ-747-MONOMER.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
[Graphical view]
PRINTSiPR00110. ALPHAAMYLASE.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparison of the genomes of two Xanthomonas pathogens with differing host specificities."
    da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P.
    , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.
    Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33913 / NCPPB 528 / LMG 568Imported.

Entry informationi

Entry nameiQ7CLU8_XANCP
AccessioniPrimary (citable) accession number: Q7CLU8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.