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O00105

- IPUA_ASPNG

UniProt

O00105 - IPUA_ASPNG

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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-KW
Complete GO annotation...

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

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

        10         20         30         40         50
MRSTGYLLTL SAAFQVAQAA VTANNSQLLT WWHNTGEINT QTPVADGNVR
60 70 80 90 100
QSGLYSVKVQ TTPASSSLYY DSFVYLAIPG NGMSDQLQYT QGYNQTQAWT
110 120 130 140 150
SFLYSHDATV KISRNGSSAN SNVVIRPTSL NFPVRYDNQS VYITVPYSPT
160 170 180 190 200
GYRFSVEFDD DLISLAPSGA RQPENALLIF ASPFENSSTK PQPGSPNSIA
210 220 230 240 250
PAPGRVLGLN TTSASTVVFN PGVYYFTGHD HMVLSSSVTW VYFAPGAYVK
260 270 280 290 300
GAVEFLSTAS EVKASGHGVL SGEQYVWYAD PDEGYQKASG ANNNGLRMWR
310 320 330 340 350
GTLGNSSQTF VLNGVTVSAP PFNSMDWSGN SLDLITCRVD DYKQVGAFYG
360 370 380 390 400
QTDGLEMYPG TILQDVFYHT DDDGLKMYYS NVTARNIVMW KESVAPVVEF
410 420 430 440 450
GWTPRNTENV LFDNVDVIHQ AYANAGNNPG IFGAVNNYLY APDGLSSNHS
460 470 480 490 500
TGNSNMTVRN ITWSNFRAEG SSSALFRINP IQNLDNISIK NVSIESFEPL
510 520 530 540 550
SINTTESWMP VWYDLNNGKQ ITVTDFSIEG FTVGNTTITA SNAASVGRID
560
GVDPAYAGSV HYID
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 29, 2014
This is version 74 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