SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O00105

- IPUA_ASPNG

UniProt

O00105 - IPUA_ASPNG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Isopullulanase
Gene
ipuA
Organism
Aspergillus niger
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 564545Isopullulanase
PRO_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...) Reviewed prediction
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...) Reviewed prediction
Glycosylationi491 – 4911N-linked (GlcNAc...)
Glycosylationi503 – 5031N-linked (GlcNAc...)
Glycosylationi535 – 5351N-linked (GlcNAc...)

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

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.

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: September 3, 2014
This is version 72 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