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P29957

- AMY_PSEHA

UniProt

P29957 - AMY_PSEHA

Protein

Alpha-amylase

Gene

amy

Organism
Pseudoalteromonas haloplanktis (Alteromonas haloplanktis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 3 (30 May 2000)
      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.1 Publication
    Binds 1 chloride ion per subunit.1 Publication

    Enzyme regulationi

    Requires chloride ions for optimal activity.1 Publication

    Temperature dependencei

    Thermolabile.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi112 – 1121Calcium
    Binding sitei113 – 1131Substrate
    Metal bindingi159 – 1591Calcium; via carbonyl oxygen
    Metal bindingi168 – 1681Calcium
    Binding sitei196 – 1961Chloride
    Binding sitei196 – 1961SubstrateBy similarity
    Active sitei198 – 1981Nucleophile1 Publication
    Metal bindingi202 – 2021Calcium; via carbonyl oxygen
    Active sitei224 – 2241Proton donor1 Publication
    Binding sitei229 – 2291Substrate; via amide nitrogenBy similarity
    Binding sitei286 – 2861Chloride
    Binding sitei287 – 2871SubstrateBy similarity
    Sitei288 – 2881Transition state stabilizerBy similarity
    Binding sitei293 – 2931Substrate
    Binding sitei324 – 3241Chloride

    GO - Molecular functioni

    1. alpha-amylase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Chloride, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP29957.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase (EC:3.2.1.1)
    Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase
    Gene namesi
    Name:amy
    OrganismiPseudoalteromonas haloplanktis (Alteromonas haloplanktis)
    Taxonomic identifieri228 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi324 – 3241K → Q: Abolishes chloride binding and reduces catalytic rate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 477453Alpha-amylasePRO_0000001328Add
    BLAST
    Propeptidei478 – 669192Removed in mature formPRO_0000001329Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 98
    Disulfide bondi144 ↔ 161
    Disulfide bondi352 ↔ 359
    Disulfide bondi426 ↔ 440

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    669
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 324
    Helixi37 – 4610
    Helixi48 – 514
    Beta strandi55 – 584
    Beta strandi67 – 693
    Helixi70 – 745
    Beta strandi75 – 773
    Beta strandi79 – 813
    Helixi88 – 10013
    Beta strandi104 – 1107
    Beta strandi112 – 1143
    Beta strandi119 – 1213
    Beta strandi126 – 1283
    Helixi137 – 1393
    Helixi150 – 1534
    Helixi155 – 1606
    Beta strandi161 – 1633
    Beta strandi167 – 1693
    Helixi174 – 19017
    Beta strandi194 – 1985
    Helixi200 – 2023
    Helixi205 – 2139
    Beta strandi215 – 2173
    Beta strandi220 – 2234
    Helixi235 – 2417
    Beta strandi242 – 2454
    Helixi247 – 25913
    Helixi262 – 2676
    Helixi270 – 2723
    Helixi277 – 2793
    Beta strandi280 – 2823
    Helixi289 – 2913
    Turni292 – 2943
    Helixi302 – 3054
    Helixi306 – 31712
    Beta strandi320 – 3278
    Beta strandi344 – 3463
    Beta strandi352 – 3576
    Helixi360 – 3623
    Helixi364 – 37512
    Turni376 – 3783
    Beta strandi383 – 3875
    Beta strandi389 – 3968
    Helixi398 – 4003
    Beta strandi401 – 4066
    Beta strandi408 – 4103
    Beta strandi415 – 4173
    Beta strandi422 – 4265
    Turni428 – 4303
    Beta strandi440 – 4423
    Beta strandi444 – 4474
    Beta strandi451 – 4544
    Beta strandi461 – 4666

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AQHX-ray2.00A25-477[»]
    1AQMX-ray1.85A25-477[»]
    1B0IX-ray2.40A25-477[»]
    1G94X-ray1.74A25-472[»]
    1G9HX-ray1.80A25-472[»]
    1JD7X-ray2.25A25-477[»]
    1JD9X-ray2.50A25-477[»]
    1KXHX-ray2.30A25-472[»]
    1L0PX-ray2.10A25-472[»]
    ProteinModelPortaliP29957.
    SMRiP29957. Positions 25-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29957.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni71 – 755Substrate binding
    Regioni201 – 2022Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    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.
    PF02806. Alpha-amylase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00110. ALPHAAMYLASE.
    SMARTiSM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P29957-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLNKIITTA GLSLGLLLPS IATATPTTFV HLFEWNWQDV AQECEQYLGP    50
    KGYAAVQVSP PNEHITGSQW WTRYQPVSYE LQSRGGNRAQ FIDMVNRCSA 100
    AGVDIYVDTL INHMAAGSGT GTAGNSFGNK SFPIYSPQDF HESCTINNSD 150
    YGNDRYRVQN CELVGLADLD TASNYVQNTI AAYINDLQAI GVKGFRFDAS 200
    KHVAASDIQS LMAKVNGSPV VFQEVIDQGG EAVGASEYLS TGLVTEFKYS 250
    TELGNTFRNG SLAWLSNFGE GWGFMPSSSA VVFVDNHDNQ RGHGGAGNVI 300
    TFEDGRLYDL ANVFMLAYPY GYPKVMSSYD FHGDTDAGGP NVPVHNNGNL 350
    ECFASNWKCE HRWSYIAGGV DFRNNTADNW AVTNWWDNTN NQISFGRGSS 400
    GHMAINKEDS TLTATVQTDM ASGQYCNVLK GELSADAKSC SGEVITVNSD 450
    GTINLNIGAW DAMAIHKNAK LNTSSASSTE SDWQRTVIFI NAQTQSGQDM 500
    FIRGGIDHAY ANANLGRNCQ TSNFECAMPI RHNNLKNVTT SPWKANDNYL 550
    DWYGIENGQS SEAEGSATDW TTNVWPAGWG AEKTVNTDGF GVTPLNIWGE 600
    HYWMLDVDMD CSKAVNGWFE LKAFIKNGQG WETAIAQDNA PYTSTNHMAQ 650
    CGKINKFEFN NSGVVIRSF 669
    Length:669
    Mass (Da):73,268
    Last modified:May 30, 2000 - v3
    Checksum:iE3DD316D92B91EB7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58627 Genomic DNA. Translation: CAA41481.1.
    PIRiS23257.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58627 Genomic DNA. Translation: CAA41481.1 .
    PIRi S23257.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AQH X-ray 2.00 A 25-477 [» ]
    1AQM X-ray 1.85 A 25-477 [» ]
    1B0I X-ray 2.40 A 25-477 [» ]
    1G94 X-ray 1.74 A 25-472 [» ]
    1G9H X-ray 1.80 A 25-472 [» ]
    1JD7 X-ray 2.25 A 25-477 [» ]
    1JD9 X-ray 2.50 A 25-477 [» ]
    1KXH X-ray 2.30 A 25-472 [» ]
    1L0P X-ray 2.10 A 25-472 [» ]
    ProteinModelPortali P29957.
    SMRi P29957. Positions 25-472.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P29957.

    Miscellaneous databases

    EvolutionaryTracei P29957.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR006048. A-amylase_b_C.
    IPR006046. Alpha_amylase.
    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.
    PF02806. Alpha-amylase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00642. Aamy. 1 hit.
    SM00632. Aamy_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23."
      Feller G., Lonhienne T., Deroanne C., Libioulle C., van Beeumen J., Gerday C.
      J. Biol. Chem. 267:5217-5221(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-64 AND 471-477.
      Strain: A23.
    2. "Characterization of the C-terminal propeptide involved in bacterial wall spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis."
      Feller G., D'Amico S., Benotmane A.M., Joly F., van Beeumen J., Gerday C.
      J. Biol. Chem. 273:12109-12115(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
      Strain: A23.
    3. "Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor."
      Aghajari N., Feller G., Gerday C., Haser R.
      Protein Sci. 7:564-572(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-477.
      Strain: A23.
    4. "Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic alpha-amylase."
      Aghajari N., Roth M., Haser R.
      Biochemistry 41:4273-4280(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 25-472 IN COMPLEX WITH OLIGOSACCHARIDE, ACTIVE SITE, DISULFIDE BONDS.
    5. "Structural basis of alpha-amylase activation by chloride."
      Aghajari N., Feller G., Gerday C., Haser R.
      Protein Sci. 11:1435-1441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-472 IN COMPLEXES WITH CALCIUM, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF LYS-324, DISULFIDE BONDS.

    Entry informationi

    Entry nameiAMY_PSEHA
    AccessioniPrimary (citable) accession number: P29957
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 95 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

    3D-structure, Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3