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P10342

- ISOA_PSEAY

UniProt

P10342 - ISOA_PSEAY

Protein

Isoamylase

Gene

iam

Organism
Pseudomonas amyloderamosa
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      Previous versions | rss
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    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 stabilizerBy similarity

    GO - Molecular functioni

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10342.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81A → G in AAA25854. (PubMed:3379068)Curated
    Sequence conflicti126 – 1261F → C in AAA25854. (PubMed:3379068)Curated
    Sequence conflicti169 – 1691G → C in AAA25854. (PubMed:3379068)Curated
    Sequence conflicti386 – 3861L → V in AAA25854. (PubMed:3379068)Curated
    Sequence conflicti413 – 4164GAYT → AVH in AAA25854. (PubMed:3379068)Curated
    Sequence conflicti555 – 5562WP → S in AAA25854. (PubMed:3379068)Curated
    Sequence conflicti658 – 6614LRPS → SPV in AAA25854. (PubMed:3379068)Curated

    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: October 1, 2014
    This is version 98 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