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P26613

- AMY2_SALTY

UniProt

P26613 - AMY2_SALTY

Protein

Cytoplasmic alpha-amylase

Gene

amyA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi104 – 1041CalciumBy similarity
    Active sitei235 – 2351NucleophileBy similarity
    Metal bindingi239 – 2391Calcium; via carbonyl oxygenBy similarity
    Active sitei265 – 2651Proton donorBy similarity
    Sitei332 – 3321Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB-EC
    2. calcium ion binding Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciSENT99287:GCTI-1974-MONOMER.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytoplasmic alpha-amylase (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    Gene namesi
    Name:amyA
    Ordered Locus Names:STM1963
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Cytoplasmic alpha-amylasePRO_0000054288Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi99287.STM1963.

    Structurei

    3D structure databases

    ProteinModelPortaliP26613.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Phylogenomic databases

    eggNOGiCOG0366.
    HOGENOMiHOG000094847.
    KOiK01176.
    OMAiRATKYGD.
    OrthoDBiEOG65QWH3.
    PhylomeDBiP26613.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR013776. A-amylase_thermo.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001021. Alph-amls_thrmst. 1 hit.
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P26613-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNPTLLQYF HWYYPDGGKL WSELAERADG LNDIGINMVW LPPACKGASG    50
    GYSVGYDTYD LFDLGEFDQK GTIATKYGDK RQLLTAIDAL KKNNIAVLLD 100
    VVVNHKMGAD EKERIRVQRV NQDDRTQIDD NIIECEGWTR YTFPARAGQY 150
    SNFIWDYHCF SGIDHIENPD EDGIFKIVND YTGDGWNDQV DDEMGNFDYL 200
    MGENIDFRNH AVTEEIKYWA RWVMEQTHCD GFRLDAVKHI PAWFYKEWIE 250
    HVQAVAPKPL FIVAEYWSHE VDKLQTYIDQ VDGKTMLFDA PLQMKFHEAS 300
    RQGAEYDMRH IFTGTLVEAD PFHAVTLVAN HDTQPLQALE APVEPWFKPL 350
    AYALILLREN GVPSVFYPDL YGASYEDSGE NGETCRVDMP VINQLDRLIL 400
    ARQRFAHGIQ TLFFDHPNCI AFSRSGTEEN PGCVVVLSNG DDGEKTLLLG 450
    DNYANKTWRD FLGNRDEYVV TNDQGEATFF CNAGSVSVWV IEDV 494
    Length:494
    Mass (Da):56,522
    Last modified:January 23, 2002 - v3
    Checksum:i5C1E862FEDD5E47C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti462 – 4621L → S in AAA27110. (PubMed:1400215)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01643 Genomic DNA. Translation: AAA27110.1.
    AE006468 Genomic DNA. Translation: AAL20875.1.
    M85241 Genomic DNA. Translation: AAA27079.1.
    L13280 Unassigned DNA. Translation: AAA71970.1.
    PIRiB45738.
    RefSeqiNP_460916.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL20875; AAL20875; STM1963.
    GeneIDi1253484.
    KEGGistm:STM1963.
    PATRICi32382487. VBISalEnt20916_2079.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01643 Genomic DNA. Translation: AAA27110.1 .
    AE006468 Genomic DNA. Translation: AAL20875.1 .
    M85241 Genomic DNA. Translation: AAA27079.1 .
    L13280 Unassigned DNA. Translation: AAA71970.1 .
    PIRi B45738.
    RefSeqi NP_460916.1. NC_003197.1.

    3D structure databases

    ProteinModelPortali P26613.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM1963.

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL20875 ; AAL20875 ; STM1963 .
    GeneIDi 1253484.
    KEGGi stm:STM1963.
    PATRICi 32382487. VBISalEnt20916_2079.

    Phylogenomic databases

    eggNOGi COG0366.
    HOGENOMi HOG000094847.
    KOi K01176.
    OMAi RATKYGD.
    OrthoDBi EOG65QWH3.
    PhylomeDBi P26613.

    Enzyme and pathway databases

    BioCyci SENT99287:GCTI-1974-MONOMER.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR013776. A-amylase_thermo.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001021. Alph-amls_thrmst. 1 hit.
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Escherichia coli produces a cytoplasmic alpha-amylase, AmyA."
      Raha M., Kawagishi I., Mueller V., Kihara M., Macnab R.M.
      J. Bacteriol. 174:6644-6652(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SJW1103.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "Subdivision of flagellar region III of the Escherichia coli and Salmonella typhimurium chromosomes and identification of two additional flagellar genes."
      Kawagishi I., Mueller V., Williams A.W., Irikura V.M., Macnab R.M.
      J. Gen. Microbiol. 138:1051-1065(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
      Strain: SJW1103.
    4. "Organization of the Escherichia coli and Salmonella typhimurium chromosomes between flagellar regions IIIa and IIIb, including a large non-coding region."
      Raha M., Kihara M., Kawagishi I., Macnab R.M.
      J. Gen. Microbiol. 139:1401-1407(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-494.

    Entry informationi

    Entry nameiAMY2_SALTY
    AccessioniPrimary (citable) accession number: P26613
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3