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P10342

- ISOA_PSEAY

UniProt

P10342 - ISOA_PSEAY

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Protein

Isoamylase

Gene
iam
Organism
Pseudomonas amyloderamosa
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins.

Cofactori

Binds 1 calcium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Calcium
Metal bindingi255 – 2551Calcium
Metal bindingi256 – 2561Calcium; via carbonyl oxygen
Metal bindingi258 – 2581Calcium
Metal bindingi285 – 2851Calcium
Active sitei401 – 4011Nucleophile
Active sitei461 – 4611Proton donor
Sitei536 – 5361Transition state stabilizer By similarity

GO - Molecular functioni

  1. isoamylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Isoamylase (EC:3.2.1.68)
Gene namesi
Name:iam
OrganismiPseudomonas amyloderamosa
Taxonomic identifieri32043 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Add
BLAST
Chaini27 – 776750IsoamylasePRO_0000001424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi410 ↔ 422
Disulfide bondi546 ↔ 616
Disulfide bondi738 ↔ 766

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By maltose.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
776
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 374
Beta strandi41 – 499
Beta strandi54 – 6613
Beta strandi70 – 745
Beta strandi82 – 887
Helixi89 – 946
Beta strandi102 – 1098
Helixi163 – 1664
Turni170 – 1745
Turni178 – 1803
Helixi202 – 2043
Beta strandi207 – 2104
Helixi212 – 2165
Helixi224 – 2263
Helixi230 – 2356
Helixi237 – 2437
Beta strandi247 – 2515
Turni259 – 2624
Helixi286 – 2883
Helixi296 – 31015
Beta strandi314 – 3196
Beta strandi328 – 3336
Helixi343 – 3519
Beta strandi358 – 3614
Beta strandi364 – 3685
Helixi376 – 39116
Beta strandi397 – 4004
Helixi403 – 4075
Beta strandi411 – 4144
Helixi437 – 4448
Beta strandi454 – 4607
Beta strandi480 – 4823
Helixi484 – 49512
Helixi504 – 5118
Helixi515 – 5184
Helixi519 – 5213
Helixi525 – 5273
Beta strandi528 – 5303
Beta strandi535 – 5373
Helixi540 – 5434
Turni572 – 5776
Helixi581 – 59717
Beta strandi598 – 6058
Helixi608 – 6103
Turni626 – 6283
Helixi636 – 65419
Helixi656 – 6583
Turni666 – 6683
Beta strandi669 – 6724
Beta strandi676 – 6783
Helixi681 – 6844
Beta strandi691 – 6966
Helixi698 – 7014
Beta strandi707 – 7126
Beta strandi714 – 7163
Beta strandi718 – 7214
Beta strandi726 – 73611
Helixi739 – 7413
Beta strandi754 – 7585
Beta strandi762 – 7654
Beta strandi767 – 77610

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BF2X-ray2.00A27-776[»]
ProteinModelPortaliP10342.
SMRiP10342. Positions 27-776.

Miscellaneous databases

EvolutionaryTraceiP10342.

Family & Domainsi

Sequence similaritiesi

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.
InterProiIPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P10342-1 [UniParc]FASTAAdd to Basket

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MKCPKILAAL LGCAVLAGVP AMPAHAAINS MSLGASYDAQ QANITFRVYS    50
SQATRIVLYL YSAGYGVQES ATYTLSPAGS GVWAVTVPVS SIKAAGITGA 100
VYYGYRAWGP NWPYASNWGK GSQAGFVSDV DANGDRFNPN KLLLDPYAQE 150
VSQDPLNPSN QNGNVFASGA SYRTTDSGIY APKGVVLVPS TQSTGTKPTR 200
AQKDDVIYEV HVRGFTEQDT SIPAQYRGTY YGAGLKASYL ASLGVTAVEF 250
LPVQETQNDA NDVVPNSDAN QNYWGYMTEN YFSPDRRYAY NKAAGGPTAE 300
FQAMVQAFHN AGIKVYMDVV YNHTAEGGTW TSSDPTTATI YSWRGLDNAT 350
YYELTSGNQY FYDNTGIGAN FNTYNTVAQN LIVDSLAYWA NTMGVDGFRF 400
DLASVLGNSC LNGAYTASAP NCPNGGYNFD AADSNVAINR ILREFTVRPA 450
AGGSGLDLFA EPWAIGGNSY QLGGFPQGWS EWNGLFRDSL RQAQNELGSM 500
TIYVTQDAND FSGSSNLFQS SGRSPWNSIN FIDVHDGMTL KDVYSCNGAN 550
NSQAWPYGPS DGGTSTNYSW DQGMSAGTGA AVDQRRAART GMAFEMLSAG 600
TPLMQGGDEY LRTLQCNNNA YNLDSSANWL TYSWTTDQSN FYTFAQRLIA 650
FRKAHPALRP SSWYSGSQLT WYQPSGAVAD SNYWNNTSNY AIAYAINGPS 700
LGDSNSIYVA YNGWSSSVTF TLPAPPSGTQ WYRVTDTCDW NDGASTFVAP 750
GSETLIGGAG TTYGQCGQSL LLLISK 776
Length:776
Mass (Da):83,627
Last modified:December 15, 1998 - v3
Checksum:iF738BF8040246169
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81A → G in AAA25854. 1 Publication
Sequence conflicti126 – 1261F → C in AAA25854. 1 Publication
Sequence conflicti169 – 1691G → C in AAA25854. 1 Publication
Sequence conflicti386 – 3861L → V in AAA25854. 1 Publication
Sequence conflicti413 – 4164GAYT → AVH in AAA25854. 1 Publication
Sequence conflicti555 – 5562WP → S in AAA25854. 1 Publication
Sequence conflicti658 – 6614LRPS → SPV in AAA25854. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03871 Genomic DNA. Translation: AAA25854.1. Frameshift.
X13378 Genomic DNA. Translation: CAA31754.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03871 Genomic DNA. Translation: AAA25854.1 . Frameshift.
X13378 Genomic DNA. Translation: CAA31754.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BF2 X-ray 2.00 A 27-776 [» ]
ProteinModelPortali P10342.
SMRi P10342. Positions 27-776.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P10342.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02922. CBM_48. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiISOA_PSEAY
AccessioniPrimary (citable) accession number: P10342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 15, 1998
Last modified: April 16, 2014
This is version 97 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

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

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