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P10342 (ISOA_PSEAY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoamylase
EC=3.2.1.68
Gene names
Name:iam
OrganismPseudomonas amyloderamosa
Taxonomic identifier32043 [NCBI]
Taxonomic lineageBacteria › Proteobacteria ›

Protein attributes

Sequence length776 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->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.

Cofactor

Binds 1 calcium ion per subunit.

Subunit structure

Monomer.

Induction

By maltose.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence caution

The sequence AAA25854.1 differs from that shown. Reason: Frameshift at positions 168, 171, 454, 479, 490, 650 and 662.

Ontologies

Keywords
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processglycogen catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionisoamylase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 776750Isoamylase
PRO_0000001424

Sites

Active site4011Nucleophile
Active site4611Proton donor
Metal binding1541Calcium
Metal binding2551Calcium
Metal binding2561Calcium; via carbonyl oxygen
Metal binding2581Calcium
Metal binding2851Calcium
Site5361Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond410 ↔ 422
Disulfide bond546 ↔ 616
Disulfide bond738 ↔ 766

Experimental info

Sequence conflict81A → G in AAA25854. Ref.1
Sequence conflict1261F → C in AAA25854. Ref.1
Sequence conflict1691G → C in AAA25854. Ref.1
Sequence conflict3861L → V in AAA25854. Ref.1
Sequence conflict413 – 4164GAYT → AVH in AAA25854. Ref.1
Sequence conflict555 – 5562WP → S in AAA25854. Ref.1
Sequence conflict658 – 6614LRPS → SPV in AAA25854. Ref.1

Secondary structure

1 ..................................................................................................................... 776
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10342 [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: F738BF8040246169

FASTA77683,627
        10         20         30         40         50         60 
MKCPKILAAL LGCAVLAGVP AMPAHAAINS MSLGASYDAQ QANITFRVYS SQATRIVLYL 

        70         80         90        100        110        120 
YSAGYGVQES ATYTLSPAGS GVWAVTVPVS SIKAAGITGA VYYGYRAWGP NWPYASNWGK 

       130        140        150        160        170        180 
GSQAGFVSDV DANGDRFNPN KLLLDPYAQE VSQDPLNPSN QNGNVFASGA SYRTTDSGIY 

       190        200        210        220        230        240 
APKGVVLVPS TQSTGTKPTR AQKDDVIYEV HVRGFTEQDT SIPAQYRGTY YGAGLKASYL 

       250        260        270        280        290        300 
ASLGVTAVEF LPVQETQNDA NDVVPNSDAN QNYWGYMTEN YFSPDRRYAY NKAAGGPTAE 

       310        320        330        340        350        360 
FQAMVQAFHN AGIKVYMDVV YNHTAEGGTW TSSDPTTATI YSWRGLDNAT YYELTSGNQY 

       370        380        390        400        410        420 
FYDNTGIGAN FNTYNTVAQN LIVDSLAYWA NTMGVDGFRF DLASVLGNSC LNGAYTASAP 

       430        440        450        460        470        480 
NCPNGGYNFD AADSNVAINR ILREFTVRPA AGGSGLDLFA EPWAIGGNSY QLGGFPQGWS 

       490        500        510        520        530        540 
EWNGLFRDSL RQAQNELGSM TIYVTQDAND FSGSSNLFQS SGRSPWNSIN FIDVHDGMTL 

       550        560        570        580        590        600 
KDVYSCNGAN NSQAWPYGPS DGGTSTNYSW DQGMSAGTGA AVDQRRAART GMAFEMLSAG 

       610        620        630        640        650        660 
TPLMQGGDEY LRTLQCNNNA YNLDSSANWL TYSWTTDQSN FYTFAQRLIA FRKAHPALRP 

       670        680        690        700        710        720 
SSWYSGSQLT WYQPSGAVAD SNYWNNTSNY AIAYAINGPS LGDSNSIYVA YNGWSSSVTF 

       730        740        750        760        770 
TLPAPPSGTQ WYRVTDTCDW NDGASTFVAP GSETLIGGAG TTYGQCGQSL LLLISK

« Hide

References

[1]"Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15."
Amemura A., Chakraborty R., Fujita M., Noumi T., Futai M.
J. Biol. Chem. 263:9271-9275(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SB-15.
[2]"Nucleotide sequence and expression of the isoamylase gene from an isoamylase-hyperproducing mutant, Pseudomonas amyloderamosa JD210."
Chen J.H., Chen Z.Y., Chow T.Y., Chen J.C., Tan S.T., Hsu W.H.
Biochim. Biophys. Acta 1087:309-315(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: JD210.
[3]"Transcription of the isoamylase gene (iam) in Pseudomonas amyloderamosa SB-15."
Amemura A., Fujita M., Futai M.
J. Bacteriol. 171:4320-4325(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 744-776.
Strain: SB-15.
[4]"Three-dimensional structure of Pseudomonas isoamylase at 2.2-A resolution."
Katsuya Y., Mezaki Y., Kubota M., Matsuura Y.
J. Mol. Biol. 281:885-897(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03871 Genomic DNA. Translation: AAA25854.1. Frameshift.
X13378 Genomic DNA. Translation: CAA31754.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF2X-ray2.00A27-776[»]
ProteinModelPortalP10342.
SMRP10342. Positions 27-776.
ModBaseSearch...

Protein family/group databases

CAZyCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR011837. Glycogen_debranch_debranch.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PTHR10357:SF74. PTHR10357:SF74. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP10342.

Entry information

Entry nameISOA_PSEAY
AccessionPrimary (citable) accession number: P10342
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 15, 1998
Last modified: April 3, 2013
This is version 93 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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