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Protein

Glucoamylase

Gene

gla-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateBy similarity
Active sitei211 – 2111Proton acceptorPROSITE-ProRule annotation
Active sitei214 – 2141Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC
  2. starch binding Source: InterPro

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:gla-1
ORF Names:B5O22.70, NCU01517
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 6, Linkage Group II

Pathology & Biotechi

Protein family/group databases

Allergomei10750. Neu cr Glucoamylase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 3516Sequence AnalysisPRO_0000001469Add
BLAST
Chaini36 – 626591GlucoamylasePRO_0000001470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU01517.1.

Structurei

3D structure databases

ProteinModelPortaliP14804.
SMRiP14804. Positions 36-626.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini520 – 626107CBM20PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3387.
HOGENOMiHOG000182646.
InParanoidiP14804.
KOiK01178.
OrthoDBiEOG7NPG4B.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFiPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSiPR00736. GLHYDRLASE15.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14804-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLVSSLLVV GAAFQAVLGL PDPLHEKRHS DIIKRSVDSY IQTETPIAQK
60 70 80 90 100
NLLCNIGASG CRASGAASGV VVASPSKSSP DYWYTWTRDA ALVTKLIVDE
110 120 130 140 150
FTNDYNTTLQ NTIQAYAAAQ AKLQGVSNPS GSLSNGAGLG EPKFMVDLQQ
160 170 180 190 200
FTGAWGRPQR DGPPLRAIAL IGYGKWLVSN GYADTAKSII WPIVKNDLAY
210 220 230 240 250
TAQYWNNTGF DLWEEVNSSS FFTIAASHRA LVEGSAFAKS VGSSCSACDA
260 270 280 290 300
IAPQILCFQQ SFWSNSGYII SNFVNYRSGK DINSVLTSIH NFDPAAGCDV
310 320 330 340 350
NTFQPCSDRA LANHKVVVDS MRFWGVNSGR TAGKAAAVGR YAEDVYYNGN
360 370 380 390 400
PWYLATLAAA EQLYDAVYVW KKQGSITVTS TSLAFFKDLV PSVSTGTYSS
410 420 430 440 450
SSSTYTAIIN AVTTYADGFV DIVAQYTPSD GSLAEQFDKD SGAPLSATHL
460 470 480 490 500
TWSYASFLSA AARRAGIVPP SWGAASANSL PGSCSASTVA GSYATATATS
510 520 530 540 550
FPANLTPAST TVTPPTQTGC AADHEVLVTF NEKVTTSYGQ TVKVVGSIAA
560 570 580 590 600
LGNWAPASGV TLSAKQYSSS NPLWSTTIAL PQGTSFKYKY VVVNSDGSVK
610 620
WENDPDRSYA VGTDCASTAT LDDTWR
Length:626
Mass (Da):66,475
Last modified:April 30, 2003 - v3
Checksum:i54E5BDDBA7A3E349
GO

Sequence cautioni

The sequence EAA27730.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821Missing in CAA47707 (PubMed:8221928).Curated
Sequence conflicti550 – 5501A → R in CAA47707 (PubMed:8221928).Curated
Sequence conflicti560 – 5601V → L in CAA47707 (PubMed:8221928).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67291 Genomic DNA. Translation: CAA47707.1.
AL355932 Genomic DNA. Translation: CAB91426.1.
CM002237 Genomic DNA. Translation: EAA27730.2. Different initiation.
PIRiS36364.
RefSeqiXP_956966.1. XM_951873.2.
UniGeneiNcr.420.

Genome annotation databases

EnsemblFungiiEFNCRT00000001634; EFNCRP00000001634; EFNCRG00000001632.
GeneIDi3873129.
KEGGincr:NCU01517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67291 Genomic DNA. Translation: CAA47707.1.
AL355932 Genomic DNA. Translation: CAB91426.1.
CM002237 Genomic DNA. Translation: EAA27730.2. Different initiation.
PIRiS36364.
RefSeqiXP_956966.1. XM_951873.2.
UniGeneiNcr.420.

3D structure databases

ProteinModelPortaliP14804.
SMRiP14804. Positions 36-626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU01517.1.

Protein family/group databases

Allergomei10750. Neu cr Glucoamylase.
CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000001634; EFNCRP00000001634; EFNCRG00000001632.
GeneIDi3873129.
KEGGincr:NCU01517.

Phylogenomic databases

eggNOGiCOG3387.
HOGENOMiHOG000182646.
InParanoidiP14804.
KOiK01178.
OrthoDBiEOG7NPG4B.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFiPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSiPR00736. GLHYDRLASE15.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the glucoamylase gene of Neurospora crassa."
    Stone P.J., Makoff A.J., Parish J.H., Radford A.
    Curr. Genet. 24:205-211(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  3. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  4. "Exported proteins of Neurospora crassa: 1-glucoamylase."
    Koh-Luar S.I., Parish J.H., Bleasby A.J., Pappin D.J.C., Ainley K., Johansen F.E., Radford A.
    Enzyme Microb. Technol. 11:692-695(1989)
    Cited for: PROTEIN SEQUENCE OF 36-65.
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiAMYG_NEUCR
AccessioniPrimary (citable) accession number: P14804
Secondary accession number(s): Q7RV62, Q9P5U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 30, 2003
Last modified: January 7, 2015
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.