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Q4WPQ9

- Q4WPQ9_ASPFU

UniProt

Q4WPQ9 - Q4WPQ9_ASPFU

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Protein

Alpha-amylase

Gene

AFUA_4G10130

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Calcium 1UniRule annotation
Metal bindingi180 – 1801Calcium 1; via carbonyl oxygenUniRule annotation
Metal bindingi193 – 1931Calcium 1UniRule annotation
Active sitei224 – 2241NucleophileUniRule annotation
Metal bindingi224 – 2241Calcium 2UniRule annotation
Metal bindingi228 – 2281Calcium 1; via carbonyl oxygenUniRule annotation
Active sitei248 – 2481Proton donorUniRule annotation
Metal bindingi248 – 2481Calcium 2UniRule annotation
Sitei315 – 3151Transition state stabilizerUniRule annotation

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Keywords - Ligandi

CalciumUniRule annotation, Metal-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
Gene namesi
ORF Names:AFUA_4G10130Imported
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)Imported
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi168 ↔ 182UniRule annotation
Disulfide bondi258 ↔ 301UniRule annotation

Keywords - PTMi

Disulfide bondUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi5085.CADAFUAP00008053.

Structurei

3D structure databases

ProteinModelPortaliQ4WPQ9.
SMRiQ4WPQ9. Positions 20-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000165530.
InParanoidiQ4WPQ9.
KOiK01176.
OMAiNQTQVED.
OrthoDBiEOG7RBZJ4.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFiPIRSF001024. Alph-amyl_fung. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Q4WPQ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHIRWSSFFL SCLAGTALAA TPAQWRSQSI YFLLTDRFAR TDGSTTASCD
60 70 80 90 100
TSARYCGGTW QGIIEQLDYI QGMGFTAIWI TPVTKQLPQD TSEGTAYHGY
110 120 130 140 150
WQQDIYSVNS NYGTADDLKA LASALHDRGM YLMVDVVANH MGYAGAGDSV
160 170 180 190 200
DYSVFNPFNS QTSFHPLCFI SNYDNQTDVE NCWLGDNSVP LPDLDTTNPD
210 220 230 240 250
VQKIWYNWVN SLVSNYSIDG LRIDTVKHVQ SDFWPGFNDA AGVYCIGEVF
260 270 280 290 300
DGDPAYTCPY QEVLDGVLNY PIYYPLLKAF QSTSGSMSSL YDMINTVKSQ
310 320 330 340 350
CADSTLLGTF VENHDTPRFA SYTKDMALAK NAAAFIIFSD GIPIIYAGQE
360 370 380 390 400
QHYSGGADPA NREAVWLSGY STTSDLYKLI ATANAIRSHA ISKDPGYVTY
410 420 430 440 450
KNNPIYKDTS TIAMRKGSDG AQIITVLSNL GASGSSYTLS LGGTGYEAGQ
460 470 480 490
QLTEMFSCTT VTVGSDKKVP VSMASGLPRV FYPTAGLNGS TVCT
Length:494
Mass (Da):53,872
Last modified:July 5, 2005 - v1
Checksum:i9B3999975976A871
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL89775.1.
RefSeqiXP_751813.1. XM_746720.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00008053; CADAFUAP00008053; CADAFUAG00008053.
GeneIDi3509344.
KEGGiafm:AFUA_4G10130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AAHF01000005 Genomic DNA. Translation: EAL89775.1 .
RefSeqi XP_751813.1. XM_746720.1.

3D structure databases

ProteinModelPortali Q4WPQ9.
SMRi Q4WPQ9. Positions 20-494.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5085.CADAFUAP00008053.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAFUAT00008053 ; CADAFUAP00008053 ; CADAFUAG00008053 .
GeneIDi 3509344.
KEGGi afm:AFUA_4G10130.

Phylogenomic databases

HOGENOMi HOG000165530.
InParanoidi Q4WPQ9.
KOi K01176.
OMAi NQTQVED.
OrthoDBi EOG7RBZJ4.

Family and domain databases

Gene3Di 2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view ]
PIRSFi PIRSF001024. Alph-amyl_fung. 1 hit.
PRINTSi PR00110. ALPHAAMYLASE.
SMARTi SM00642. Aamy. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.
    , Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H., Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100Imported.

Entry informationi

Entry nameiQ4WPQ9_ASPFU
AccessioniPrimary (citable) accession number: Q4WPQ9
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2005
Last sequence update: July 5, 2005
Last modified: October 29, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3