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Reviewed, UniProtKB/Swiss-Prot P13507 (AMT4_PSEST)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glucan 1,4-alpha-maltotetraohydrolase
      Short name=G4-amylase
    EC=3.2.1.60
Alternative name(s):
    Maltotetraose-forming amylase
    Exo-maltotetraohydrolase
    Maltotetraose-forming exo-amylase
Gene names
Name: amyP
OrganismPseudomonas stutzeri (Pseudomonas perfectomarina)
Taxonomic identifier316 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

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Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 calcium ions per subunit.

Pathway

Glycan degradation; starch degradation.

Subunit structure

Monomer.

Subcellular location

Secreted.

Miscellaneous

There are several isoenzyme forms of this protein.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

glucan 1,4-alpha-maltotetraohydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 548527Glucan 1,4-alpha-maltotetraohydrolase
PRO_0000001420

Regions

Domain446 – 548103CBM20

Sites

Active site2141Nucleophile
Active site2401Proton donor
Active site3151
Metal binding221Calcium 2
Metal binding231Calcium 2; via carbonyl oxygen
Metal binding341Calcium 2
Metal binding371Calcium 2
Metal binding381Calcium 2
Metal binding1371Calcium 1
Metal binding1721Calcium 1
Metal binding1751Calcium 1; via carbonyl oxygen
Metal binding1831Calcium 1
Metal binding2181Calcium 1; via carbonyl oxygen

Amino acid modifications

Disulfide bond161 ↔ 171
Disulfide bond237 ↔ 272

Experimental info

Sequence conflict286 – 30217GSIAD…NPDPR → ARSPTGSTPERQSRPA AA sequence Ref.1

Secondary structure

1 ............................................................................. 548
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P13507-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 2B87217B3379158F

FASTA54859,876
        10         20         30         40         50         60 
MSHILRAAVL AAMLLPLPSM ADQAGKSPNA VRYHGGDEII LQGFHWNVVR EAPNDWYNIL 

        70         80         90        100        110        120 
RQQAATIAAD GFSAIWMPVP WRDFSSWSDG SKSGGGEGYF WHDFNKNGRY GSDAQLRQAA 

       130        140        150        160        170        180 
SALGGAGVKV LYDVVPNHMN RGYPDKEINL PAGQGFWRND CADPGNYPND CDDGDRFIGG 

       190        200        210        220        230        240 
DADLNTGHPQ VYGMFRDEFT NLRSQYGAGG FRFDFVRGYA PERVNSWMTD SADNSFCVGE 

       250        260        270        280        290        300 
LWKGPSEYPN WDWRNTASWQ QIIKDWSDRA KCPVFDFALK ERMQNGSIAD WKHGLNGNPD 

       310        320        330        340        350        360 
PRWREVAVTF VDNHDTGYSP GQNGGQHHWA LQDGLIRQAY AYILTSPGTP VVYWSHMYDW 

       370        380        390        400        410        420 
GYGDFIRQLI QVRRAAGVRA DSAISFHSGY SGLVATVSGS QQTLVVALNS DLGNPGQVAS 

       430        440        450        460        470        480 
GSFSEAVNAS NGQVRVWRSG TGSGGGEPGA LVSVSFRCDN GATQMGDSVY AVGNVSQLGN 

       490        500        510        520        530        540 
WSPAAALRLT DTSGYPTWKG SIALPAGQNE EWKCLIRNEA NATQVRQWQG GANNSLTPSE 


GATTVGRL

« Hide

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References

[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: 2646279] [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: 9126844] [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: 9281429] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT GLN-240.
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: 10556241] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF VARIANTS.
Strain: MO-19.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M24516 Genomic DNA. Translation: AAA25707.1.
PIRA32803.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GCYX-ray1.60A22-548[»]
1JDAX-ray2.20A22-450[»]
1JDCX-ray1.90A22-450[»]
1JDDX-ray1.90A22-450[»]
1QI3X-ray2.00A22-450[»]
1QI4X-ray2.00A22-450[»]
1QI5X-ray2.00A22-450[»]
1QPKX-ray2.00A22-439[»]
2AMGX-ray2.00A22-439[»]
ModBaseSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH13. Glycoside Hydrolase Family 13.

Enzyme and pathway databases

BRENDA3.2.1.60. 421.

Family and domain databases

InterProIPR015165. DUF1921.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat.
IPR002044. Glyco_hydro_carb-bd.
IPR013781. Glyco_hydro_sg_catalytic.
IPR013783. Ig-like_fold.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF00686. CBM_20. 1 hit.
PF09081. DUF1921. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
ProDomPD001568. Glyco_hydro_CBD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMT4_PSEST
AccessionPrimary (citable) accession number: P13507
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents