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P13507

- AMT4_PSEST

UniProt

P13507 - AMT4_PSEST

Protein

Glucan 1,4-alpha-maltotetraohydrolase

Gene

amyP

Organism
Pseudomonas stutzeri (Pseudomonas perfectomarina)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.

    Cofactori

    Binds 2 calcium ions per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi22 – 221Calcium 1
    Metal bindingi23 – 231Calcium 1; via carbonyl oxygen
    Metal bindingi34 – 341Calcium 1
    Metal bindingi37 – 371Calcium 1
    Metal bindingi38 – 381Calcium 1
    Metal bindingi137 – 1371Calcium 2
    Binding sitei138 – 1381Substrate
    Metal bindingi172 – 1721Calcium 2
    Metal bindingi175 – 1751Calcium 2; via carbonyl oxygen
    Metal bindingi183 – 1831Calcium 2
    Binding sitei212 – 2121Substrate
    Active sitei214 – 2141Nucleophile1 Publication
    Metal bindingi218 – 2181Calcium 2; via carbonyl oxygen
    Active sitei240 – 2401Proton donor1 Publication
    Binding sitei314 – 3141Substrate
    Sitei315 – 3151Transition state stabilizerBy similarity
    Binding sitei326 – 3261Substrate

    GO - Molecular functioni

    1. glucan 1,4-alpha-maltotetraohydrolase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. starch binding Source: InterPro

    GO - Biological processi

    1. starch catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00153.

    Protein family/group databases

    CAZyiCBM20. Carbohydrate-Binding Module Family 20.
    GH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucan 1,4-alpha-maltotetraohydrolase (EC:3.2.1.60)
    Short name:
    G4-amylase
    Alternative name(s):
    Exo-maltotetraohydrolase
    Maltotetraose-forming amylase
    Maltotetraose-forming exo-amylase
    Gene namesi
    Name:amyP
    OrganismiPseudomonas stutzeri (Pseudomonas perfectomarina)
    Taxonomic identifieri316 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 548527Glucan 1,4-alpha-maltotetraohydrolasePRO_0000001420Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi161 ↔ 1711 Publication
    Disulfide bondi237 ↔ 2721 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    548
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 363
    Beta strandi40 – 423
    Helixi48 – 514
    Turni53 – 553
    Helixi56 – 6914
    Beta strandi73 – 775
    Beta strandi87 – 893
    Beta strandi92 – 943
    Beta strandi102 – 1043
    Beta strandi108 – 1103
    Helixi113 – 12513
    Beta strandi129 – 1346
    Beta strandi152 – 1554
    Helixi158 – 1603
    Beta strandi165 – 1673
    Beta strandi172 – 1743
    Beta strandi180 – 1845
    Helixi189 – 20517
    Beta strandi208 – 2147
    Helixi216 – 2183
    Helixi221 – 23111
    Beta strandi235 – 2395
    Helixi245 – 2473
    Helixi253 – 2564
    Helixi259 – 27012
    Helixi277 – 2859
    Helixi288 – 2936
    Helixi295 – 2973
    Helixi301 – 3044
    Beta strandi307 – 3093
    Turni314 – 3163
    Helixi322 – 3243
    Helixi333 – 3353
    Helixi336 – 34510
    Beta strandi346 – 3538
    Helixi354 – 3585
    Helixi363 – 37614
    Beta strandi383 – 3864
    Beta strandi390 – 3989
    Beta strandi403 – 4097
    Helixi415 – 4173
    Beta strandi424 – 4296
    Turni430 – 4334
    Beta strandi434 – 4385

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GCYX-ray1.60A22-548[»]
    1JDAX-ray2.20A22-450[»]
    1JDCX-ray1.90A22-450[»]
    1JDDX-ray1.90A22-450[»]
    1QI3X-ray2.00A22-450[»]
    1QI4X-ray2.00A22-439[»]
    1QI5X-ray2.00A22-439[»]
    1QPKX-ray2.00A22-439[»]
    2AMGX-ray2.00A22-439[»]
    ProteinModelPortaliP13507.
    SMRiP13507. Positions 22-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13507.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini446 – 548103CBM20PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1002Substrate bindingBy similarity
    Regioni177 – 1815Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated
    Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR006046. Alpha_amylase.
    IPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR015165. DUF1921.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF00686. CBM_20. 1 hit.
    PF09081. DUF1921. 1 hit.
    [Graphical view]
    PRINTSiPR00110. ALPHAAMYLASE.
    SMARTiSM01065. CBM_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49452. SSF49452. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEiPS51166. CBM20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13507-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHILRAAVL AAMLLPLPSM ADQAGKSPNA VRYHGGDEII LQGFHWNVVR    50
    EAPNDWYNIL RQQAATIAAD GFSAIWMPVP WRDFSSWSDG SKSGGGEGYF 100
    WHDFNKNGRY GSDAQLRQAA SALGGAGVKV LYDVVPNHMN RGYPDKEINL 150
    PAGQGFWRND CADPGNYPND CDDGDRFIGG DADLNTGHPQ VYGMFRDEFT 200
    NLRSQYGAGG FRFDFVRGYA PERVNSWMTD SADNSFCVGE LWKGPSEYPN 250
    WDWRNTASWQ QIIKDWSDRA KCPVFDFALK ERMQNGSIAD WKHGLNGNPD 300
    PRWREVAVTF VDNHDTGYSP GQNGGQHHWA LQDGLIRQAY AYILTSPGTP 350
    VVYWSHMYDW GYGDFIRQLI QVRRAAGVRA DSAISFHSGY SGLVATVSGS 400
    QQTLVVALNS DLGNPGQVAS GSFSEAVNAS NGQVRVWRSG TGSGGGEPGA 450
    LVSVSFRCDN GATQMGDSVY AVGNVSQLGN WSPAAALRLT DTSGYPTWKG 500
    SIALPAGQNE EWKCLIRNEA NATQVRQWQG GANNSLTPSE GATTVGRL 548
    Length:548
    Mass (Da):59,876
    Last modified:November 1, 1997 - v2
    Checksum:i2B87217B3379158F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti286 – 30217GSIAD…NPDPR → ARSPTGSTPERQSRPA AA sequence (PubMed:2646279)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24516 Genomic DNA. Translation: AAA25707.1.
    PIRiA32803.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24516 Genomic DNA. Translation: AAA25707.1 .
    PIRi A32803.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GCY X-ray 1.60 A 22-548 [» ]
    1JDA X-ray 2.20 A 22-450 [» ]
    1JDC X-ray 1.90 A 22-450 [» ]
    1JDD X-ray 1.90 A 22-450 [» ]
    1QI3 X-ray 2.00 A 22-450 [» ]
    1QI4 X-ray 2.00 A 22-439 [» ]
    1QI5 X-ray 2.00 A 22-439 [» ]
    1QPK X-ray 2.00 A 22-439 [» ]
    2AMG X-ray 2.00 A 22-439 [» ]
    ProteinModelPortali P13507.
    SMRi P13507. Positions 22-439.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM20. Carbohydrate-Binding Module Family 20.
    GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00153 .

    Miscellaneous databases

    EvolutionaryTracei P13507.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR006046. Alpha_amylase.
    IPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR015165. DUF1921.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF00686. CBM_20. 1 hit.
    PF09081. DUF1921. 1 hit.
    [Graphical view ]
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM01065. CBM_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49452. SSF49452. 1 hit.
    SSF51445. SSF51445. 1 hit.
    PROSITEi PS51166. CBM20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19."
      Fujita M., Torigoe K., Nakada T., Tsusaki K., Kubota M., Sakai S., Tsujisaka Y.
      J. Bacteriol. 171:1333-1339(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: MO-19.
    2. "Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri."
      Morishita Y., Hasegawa K., Matsuura Y., Katsube Y., Kubota M., Sakai S.
      J. Mol. Biol. 267:661-672(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 286-302.
      Strain: MO-19.
    3. "Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose."
      Yoshioka Y., Hasegawa K., Matsuura Y., Katsube Y., Kubota M.
      J. Mol. Biol. 271:619-628(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT GLN-240 IN COMPLEX WITH MALTOPENTAOSE, CALCIUM IONS.
      Strain: MO-19.
    4. "Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase."
      Hasegawa K., Kubota M., Matsuura Y.
      Protein Eng. 12:819-824(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF VARIANTS IN COMPLEXES WITH CALCIUM IONS AND MALTOTETRAOSE, DISULFIDE BONDS, ACTIVE SITE.
      Strain: MO-19.

    Entry informationi

    Entry nameiAMT4_PSEST
    AccessioniPrimary (citable) accession number: P13507
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are several isoenzyme forms of this protein.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

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

    External Data

    Dasty 3