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Protein

Isopullulanase

Gene

ipuA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.57. 518.

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000002152020 – 564IsopullulanaseAdd BLAST545

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi24N-linked (GlcNAc...)1
Glycosylationi94N-linked (GlcNAc...)1
Glycosylationi115N-linked (GlcNAc...)1
Glycosylationi138N-linked (GlcNAc...)1
Glycosylationi186N-linked (GlcNAc...)Sequence analysis1
Glycosylationi210N-linked (GlcNAc...)1
Glycosylationi305N-linked (GlcNAc...)1
Glycosylationi381N-linked (GlcNAc...)1
Glycosylationi448N-linked (GlcNAc...)1
Glycosylationi455N-linked (GlcNAc...)1
Glycosylationi460N-linked (GlcNAc...)1
Glycosylationi486N-linked (GlcNAc...)Sequence analysis1
Glycosylationi491N-linked (GlcNAc...)1
Glycosylationi503N-linked (GlcNAc...)1
Glycosylationi535N-linked (GlcNAc...)1

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1564
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 29Combined sources6
Beta strandi36 – 38Combined sources3
Beta strandi40 – 42Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi56 – 63Combined sources8
Beta strandi70 – 72Combined sources3
Beta strandi75 – 77Combined sources3
Helixi79 – 82Combined sources4
Helixi84 – 89Combined sources6
Beta strandi96 – 106Combined sources11
Beta strandi108 – 113Combined sources6
Beta strandi123 – 127Combined sources5
Helixi128 – 130Combined sources3
Beta strandi134 – 137Combined sources4
Beta strandi140 – 145Combined sources6
Beta strandi152 – 158Combined sources7
Helixi159 – 161Combined sources3
Beta strandi162 – 165Combined sources4
Turni166 – 169Combined sources4
Beta strandi170 – 182Combined sources13
Turni187 – 189Combined sources3
Beta strandi196 – 199Combined sources4
Beta strandi203 – 205Combined sources3
Turni209 – 211Combined sources3
Beta strandi215 – 219Combined sources5
Beta strandi221 – 225Combined sources5
Beta strandi232 – 234Combined sources3
Beta strandi240 – 243Combined sources4
Beta strandi247 – 251Combined sources5
Beta strandi253 – 255Combined sources3
Beta strandi259 – 267Combined sources9
Beta strandi269 – 271Combined sources3
Helixi281 – 283Combined sources3
Helixi289 – 291Combined sources3
Beta strandi298 – 302Combined sources5
Beta strandi308 – 314Combined sources7
Beta strandi316 – 318Combined sources3
Beta strandi324 – 328Combined sources5
Helixi332 – 334Combined sources3
Beta strandi335 – 345Combined sources11
Beta strandi349 – 351Combined sources3
Beta strandi362 – 372Combined sources11
Beta strandi379 – 391Combined sources13
Beta strandi393 – 395Combined sources3
Beta strandi397 – 399Combined sources3
Beta strandi407 – 419Combined sources13
Helixi425 – 427Combined sources3
Beta strandi431 – 434Combined sources4
Turni438 – 440Combined sources3
Beta strandi452 – 472Combined sources21
Beta strandi475 – 478Combined sources4
Beta strandi481 – 497Combined sources17
Helixi500 – 502Combined sources3
Beta strandi507 – 509Combined sources3
Turni515 – 517Combined sources3
Beta strandi523 – 533Combined sources11
Turni540 – 547Combined sources8
Beta strandi549 – 552Combined sources4
Turni554 – 556Combined sources3
Helixi557 – 559Combined sources3
Beta strandi560 – 563Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WMRX-ray2.40A/B20-564[»]
1X0CX-ray1.70A/B20-564[»]
2Z8GX-ray1.70A/B20-564[»]
3WWGX-ray2.20A/B/C/D20-564[»]
ProteinModelPortaliO00105.
SMRiO00105.
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:
EMBLi
GenBanki
DDBJi
Links Updated
AB001940 Genomic DNA. Translation: BAA19473.1.
D85240 Genomic DNA. Translation: BAA18971.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001940 Genomic DNA. Translation: BAA19473.1.
D85240 Genomic DNA. Translation: BAA18971.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WMRX-ray2.40A/B20-564[»]
1X0CX-ray1.70A/B20-564[»]
2Z8GX-ray1.70A/B20-564[»]
3WWGX-ray2.20A/B/C/D20-564[»]
ProteinModelPortaliO00105.
SMRiO00105.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH49. Glycoside Hydrolase Family 49.
mycoCLAPiIPU49A_ASPNG.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.57. 518.

Miscellaneous databases

EvolutionaryTraceiO00105.

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.
ProtoNetiSearch...

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: November 2, 2016
This is version 82 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.