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P13507 (AMT4_PSEST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

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

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.

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_processstarch catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucan 1,4-alpha-maltotetraohydrolase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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
Region99 – 1002Substrate binding By similarity
Region177 – 1815Substrate binding

Sites

Active site2141Nucleophile Ref.4
Active site2401Proton donor Ref.4
Metal binding221Calcium 1
Metal binding231Calcium 1; via carbonyl oxygen
Metal binding341Calcium 1
Metal binding371Calcium 1
Metal binding381Calcium 1
Metal binding1371Calcium 2
Metal binding1721Calcium 2
Metal binding1751Calcium 2; via carbonyl oxygen
Metal binding1831Calcium 2
Metal binding2181Calcium 2; via carbonyl oxygen
Binding site1381Substrate
Binding site2121Substrate
Binding site3141Substrate
Binding site3261Substrate
Site3151Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond161 ↔ 171 Ref.4
Disulfide bond237 ↔ 272 Ref.4

Experimental info

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P13507 [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

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] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M24516 Genomic DNA. Translation: AAA25707.1.
PIRA32803.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP13507.
SMRP13507. Positions 22-439.
ModBaseSearch...

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00153.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006046. 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]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF00686. CBM_20. 1 hit.
PF09081. DUF1921. 1 hit.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF49452. CBD_4. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13507.

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: April 3, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

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