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G5EB45

- G5EB45_EMENI

UniProt

G5EB45 - G5EB45_EMENI

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Protein

Alpha-amylase

Gene

AN2018.2

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
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 bindingi134 – 1341Calcium 1UniRule annotation
Metal bindingi175 – 1751Calcium 1; via carbonyl oxygenUniRule annotation
Metal bindingi188 – 1881Calcium 1UniRule annotation
Active sitei219 – 2191NucleophileUniRule annotation
Metal bindingi219 – 2191Calcium 2UniRule annotation
Metal bindingi223 – 2231Calcium 1; via carbonyl oxygenUniRule annotation
Active sitei243 – 2431Proton donorUniRule annotation
Metal bindingi243 – 2431Calcium 2UniRule annotation
Sitei310 – 3101Transition 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 annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolismUniRule annotation

Keywords - Ligandi

CalciumUniRule annotation, Metal-bindingUniRule annotation

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylaseUniRule annotation (EC:3.2.1.1UniRule annotation)
Gene namesi
ORF Names:AN2018.2Imported, ANIA_02018Imported
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)Imported
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560: Chromosome VII

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi163 ↔ 177UniRule annotation
Disulfide bondi253 ↔ 296UniRule annotation

Keywords - PTMi

Disulfide bondUniRule annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000165530.
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.

G5EB45-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSPLFLSFA ATVLAATPAE WRSQSIYFLL TDRFARTDNS TTAECDTSAK
60 70 80 90 100
YCGGTWQGII NQLDYIQGMG FTAIWITPVT ANLEDGQHGE AYHGYWQQDI
110 120 130 140 150
YALNPHFGTQ DDLRALSDAL HDRGMYLMVD VVANHFGYDA PAASVDYSAF
160 170 180 190 200
NPFNSADYFH TPCDITDYDN QTQVEDCWLY TDAVSLPDVD TTNEEVKEIW
210 220 230 240 250
YDWVGDLVSD YSIDGLRIDT ARHVQKDFWR DYNDAAGVYC VGEVFQGDPD
260 270 280 290 300
YTCGYQEVMD GVLNYPIYYP LLRAFSSTSG SLSDLANMIE TVKYTCSDAT
310 320 330 340 350
LLGNFIENHD NPRFASYTDD ISLAKNVAAF VILSDGIPII YAGQEQHYSG
360 370 380 390 400
AGDPANREAT WLSGYDSTSE LYQFISKTNQ IRNHAIWQNE TYLSYKNYAI
410 420 430 440 450
YNENNVLAMR KGFDGSQIIT ILTNAGADAG SSTVSVPNTG FTAGAAVTEI
460 470 480 490
YTCEDITVSG SGEVSVPMES GLPRVLYPKA KLEGSGICGL
Length:490
Mass (Da):54,250
Last modified:December 14, 2011 - v1
Checksum:iA891C4ACEAEB5305
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BN001307 Genomic DNA. Translation: CBF86021.1.
AACD01000032 Genomic DNA. Translation: EAA64850.1.
RefSeqiXP_659622.1. XM_654530.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008686; CADANIAP00008686; CADANIAG00008686.
GeneIDi2875021.
KEGGiani:AN2018.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BN001307 Genomic DNA. Translation: CBF86021.1 .
AACD01000032 Genomic DNA. Translation: EAA64850.1 .
RefSeqi XP_659622.1. XM_654530.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00008686 ; CADANIAP00008686 ; CADANIAG00008686 .
GeneIDi 2875021.
KEGGi ani:AN2018.2.

Phylogenomic databases

HOGENOMi HOG000165530.
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

« Hide 'large scale' publications
  1. Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H., Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T., Blitshsteyn B.
    , Bloom T., Blye J., Boguslavskiy L., Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J., Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T., Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S., Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P., Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G., Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A., Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J., Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S., Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C., Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S., Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FGSC A4.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4Imported and FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139Imported.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139Imported.
  4. "The 2008 update of the Aspergillus nidulans genome annotation: A community effort."
    Russo Wortman J., Mabey Gilsenan J., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J.M., Durek P., Espeso E., Fekete E., Flipphi M., Garcia Estrada C.
    , Geysens S., Goldman G., de Groot P.W.J., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A.K.W., Kim J-M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., MacCabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Posci I., Punt P.J., Ram A.F.J., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van der Vondervoot P.J.I., de Vries R.P., Walton J., Xiang X., Xiong Y., Ping Zeng A., Brandt B.W., Cornell M.J., van den Hondel C.A.M.J.J., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-S13(2009)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: FGSC A4Imported.

Entry informationi

Entry nameiG5EB45_EMENI
AccessioniPrimary (citable) accession number: G5EB45
Secondary accession number(s): C8VLE6
Entry historyi
Integrated into UniProtKB/TrEMBL: December 14, 2011
Last sequence update: December 14, 2011
Last modified: October 29, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3