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O00105

- IPUA_ASPNG

UniProt

O00105 - IPUA_ASPNG

Protein

Isopullulanase

Gene

ipuA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Hydrolyzes pullulan, a linear polymer which is composed of maltotriose units with alpha-1,6 glucosidic linkages, to produce isopanose (Glca1-4Glca1-6Glc).

    Catalytic activityi

    Hydrolysis of pullulan to isopanose (6-alpha-maltosylglucose).

    GO - Molecular functioni

    1. isopullulanase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH49. Glycoside Hydrolase Family 49.
    mycoCLAPiIPU49A_ASPNG.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isopullulanase (EC:3.2.1.57)
    Gene namesi
    Name:ipuA
    OrganismiAspergillus niger
    Taxonomic identifieri5061 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 564545IsopullulanasePRO_0000021520Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)
    Glycosylationi94 – 941N-linked (GlcNAc...)
    Glycosylationi115 – 1151N-linked (GlcNAc...)
    Glycosylationi138 – 1381N-linked (GlcNAc...)
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi210 – 2101N-linked (GlcNAc...)
    Glycosylationi305 – 3051N-linked (GlcNAc...)
    Glycosylationi381 – 3811N-linked (GlcNAc...)
    Glycosylationi448 – 4481N-linked (GlcNAc...)
    Glycosylationi455 – 4551N-linked (GlcNAc...)
    Glycosylationi460 – 4601N-linked (GlcNAc...)
    Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi491 – 4911N-linked (GlcNAc...)
    Glycosylationi503 – 5031N-linked (GlcNAc...)
    Glycosylationi535 – 5351N-linked (GlcNAc...)

    Post-translational modificationi

    N-glycosylated.

    Keywords - PTMi

    Glycoprotein

    Structurei

    Secondary structure

    1
    564
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 296
    Beta strandi36 – 383
    Beta strandi40 – 423
    Beta strandi49 – 513
    Beta strandi56 – 638
    Beta strandi70 – 723
    Beta strandi75 – 773
    Helixi79 – 824
    Helixi84 – 896
    Beta strandi96 – 10611
    Beta strandi108 – 1136
    Beta strandi123 – 1275
    Helixi128 – 1303
    Beta strandi134 – 1374
    Beta strandi140 – 1456
    Beta strandi152 – 1587
    Helixi159 – 1613
    Beta strandi162 – 1654
    Turni166 – 1694
    Beta strandi170 – 18213
    Turni187 – 1893
    Beta strandi196 – 1994
    Beta strandi203 – 2053
    Turni209 – 2113
    Beta strandi215 – 2195
    Beta strandi221 – 2255
    Beta strandi232 – 2343
    Beta strandi240 – 2434
    Beta strandi247 – 2515
    Beta strandi253 – 2553
    Beta strandi259 – 2679
    Beta strandi269 – 2713
    Helixi281 – 2833
    Helixi289 – 2913
    Beta strandi298 – 3025
    Beta strandi308 – 3147
    Beta strandi316 – 3183
    Beta strandi324 – 3285
    Helixi332 – 3343
    Beta strandi335 – 34511
    Beta strandi349 – 3513
    Beta strandi362 – 37211
    Beta strandi379 – 39113
    Beta strandi393 – 3953
    Beta strandi397 – 3993
    Beta strandi407 – 41913
    Helixi425 – 4273
    Beta strandi431 – 4344
    Turni438 – 4403
    Beta strandi452 – 47221
    Beta strandi475 – 4784
    Beta strandi481 – 49717
    Helixi500 – 5023
    Beta strandi507 – 5093
    Turni515 – 5173
    Beta strandi523 – 53311
    Turni540 – 5478
    Beta strandi549 – 5524
    Turni554 – 5563
    Helixi557 – 5593
    Beta strandi560 – 5634

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WMRX-ray2.40A/B20-564[»]
    1X0CX-ray1.70A/B20-564[»]
    2Z8GX-ray1.70A/B20-564[»]
    ProteinModelPortaliO00105.
    SMRiO00105. Positions 20-564.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00105.

    Family & Domainsi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.160.20.10. 1 hit.
    2.60.350.10. 1 hit.
    InterProiIPR005192. Glyco_hydro_49.
    IPR023226. Glyco_hydro_49_N_dom.
    IPR012334. Pectin_lyas_fold.
    IPR011050. Pectin_lyase_fold/virulence.
    [Graphical view]
    PfamiPF03718. Glyco_hydro_49. 1 hit.
    [Graphical view]
    SUPFAMiSSF101596. SSF101596. 1 hit.
    SSF51126. SSF51126. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O00105-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSTGYLLTL SAAFQVAQAA VTANNSQLLT WWHNTGEINT QTPVADGNVR    50
    QSGLYSVKVQ TTPASSSLYY DSFVYLAIPG NGMSDQLQYT QGYNQTQAWT 100
    SFLYSHDATV KISRNGSSAN SNVVIRPTSL NFPVRYDNQS VYITVPYSPT 150
    GYRFSVEFDD DLISLAPSGA RQPENALLIF ASPFENSSTK PQPGSPNSIA 200
    PAPGRVLGLN TTSASTVVFN PGVYYFTGHD HMVLSSSVTW VYFAPGAYVK 250
    GAVEFLSTAS EVKASGHGVL SGEQYVWYAD PDEGYQKASG ANNNGLRMWR 300
    GTLGNSSQTF VLNGVTVSAP PFNSMDWSGN SLDLITCRVD DYKQVGAFYG 350
    QTDGLEMYPG TILQDVFYHT DDDGLKMYYS NVTARNIVMW KESVAPVVEF 400
    GWTPRNTENV LFDNVDVIHQ AYANAGNNPG IFGAVNNYLY APDGLSSNHS 450
    TGNSNMTVRN ITWSNFRAEG SSSALFRINP IQNLDNISIK NVSIESFEPL 500
    SINTTESWMP VWYDLNNGKQ ITVTDFSIEG FTVGNTTITA SNAASVGRID 550
    GVDPAYAGSV HYID 564
    Length:564
    Mass (Da):61,449
    Last modified:July 1, 1997 - v1
    Checksum:iB6C0B70BF737CC40
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001940 Genomic DNA. Translation: BAA19473.1.
    D85240 Genomic DNA. Translation: BAA18971.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001940 Genomic DNA. Translation: BAA19473.1 .
    D85240 Genomic DNA. Translation: BAA18971.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WMR X-ray 2.40 A/B 20-564 [» ]
    1X0C X-ray 1.70 A/B 20-564 [» ]
    2Z8G X-ray 1.70 A/B 20-564 [» ]
    ProteinModelPortali O00105.
    SMRi O00105. Positions 20-564.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH49. Glycoside Hydrolase Family 49.
    mycoCLAPi IPU49A_ASPNG.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei O00105.

    Family and domain databases

    Gene3Di 2.160.20.10. 1 hit.
    2.60.350.10. 1 hit.
    InterProi IPR005192. Glyco_hydro_49.
    IPR023226. Glyco_hydro_49_N_dom.
    IPR012334. Pectin_lyas_fold.
    IPR011050. Pectin_lyase_fold/virulence.
    [Graphical view ]
    Pfami PF03718. Glyco_hydro_49. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101596. SSF101596. 1 hit.
    SSF51126. SSF51126. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and heterologous expression of the isopullulanase gene from Aspergillus niger ATCC 9642."
      Aoki H., Yopi X., Sakano Y.
      Biochem. J. 323:757-764(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 9642 / CBS 246.65 / DSM 63263 / IFO 6342 / NRRL 3536.
    2. "Two components of cell-bound isopullulanase from Aspergillus niger ATCC 9642 -- their purification and enzymatic properties."
      Aoki H., Yopi X., Padmajanti A., Sakano Y.
      Biosci. Biotechnol. Biochem. 60:1795-1798(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-29, CHARACTERIZATION.
      Strain: ATCC 9642 / CBS 246.65 / DSM 63263 / IFO 6342 / NRRL 3536.

    Entry informationi

    Entry nameiIPUA_ASPNG
    AccessioniPrimary (citable) accession number: O00105
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 2002
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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

    External Data

    Dasty 3