P14804 (AMYG_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucoamylase
EC=3.2.1.3

Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase

Gene names

Name:	gla-1
ORF Names:	B5O22.70, NCU01517

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) [Reference proteome]

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora › Neurospora crassa

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Sequence similarities	Belongs to the glycosyl hydrolase 15 family. Contains 1 CBM20 (carbohydrate binding type-20) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Cleavage on pair of basic residues Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	glucan 1,4-alpha-glucosidase activity Inferred from electronic annotation. Source: EC starch binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 35	16	Potential		PRO_0000001469
	Chain	36 – 626	591	Glucoamylase		PRO_0000001470
Regions
	Domain	520 – 626	107	CBM20
Sites
	Active site	211	1	Proton acceptor By similarity
	Active site	214	1	Proton donor By similarity
	Binding site	155	1	Substrate By similarity
Amino acid modifications
	Glycosylation	106	1	N-linked (GlcNAc...) Potential
	Glycosylation	206	1	N-linked (GlcNAc...) Potential
	Glycosylation	217	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	82	1	Missing in CAA47707. Ref.1
	Sequence conflict	550	1	A → R in CAA47707. Ref.1
	Sequence conflict	560	1	V → L in CAA47707. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P14804 [UniParc]. Last modified April 30, 2003. Version 3. Checksum: 54E5BDDBA7A3E349	FASTA	626	66,475
	10 20 30 40 50 60 MHLVSSLLVV GAAFQAVLGL PDPLHEKRHS DIIKRSVDSY IQTETPIAQK NLLCNIGASG 70 80 90 100 110 120 CRASGAASGV VVASPSKSSP DYWYTWTRDA ALVTKLIVDE FTNDYNTTLQ NTIQAYAAAQ 130 140 150 160 170 180 AKLQGVSNPS GSLSNGAGLG EPKFMVDLQQ FTGAWGRPQR DGPPLRAIAL IGYGKWLVSN 190 200 210 220 230 240 GYADTAKSII WPIVKNDLAY TAQYWNNTGF DLWEEVNSSS FFTIAASHRA LVEGSAFAKS 250 260 270 280 290 300 VGSSCSACDA IAPQILCFQQ SFWSNSGYII SNFVNYRSGK DINSVLTSIH NFDPAAGCDV 310 320 330 340 350 360 NTFQPCSDRA LANHKVVVDS MRFWGVNSGR TAGKAAAVGR YAEDVYYNGN PWYLATLAAA 370 380 390 400 410 420 EQLYDAVYVW KKQGSITVTS TSLAFFKDLV PSVSTGTYSS SSSTYTAIIN AVTTYADGFV 430 440 450 460 470 480 DIVAQYTPSD GSLAEQFDKD SGAPLSATHL TWSYASFLSA AARRAGIVPP SWGAASANSL 490 500 510 520 530 540 PGSCSASTVA GSYATATATS FPANLTPAST TVTPPTQTGC AADHEVLVTF NEKVTTSYGQ 550 560 570 580 590 600 TVKVVGSIAA LGNWAPASGV TLSAKQYSSS NPLWSTTIAL PQGTSFKYKY VVVNSDGSVK 610 620 WENDPDRSYA VGTDCASTAT LDDTWR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X67291 Genomic DNA. Translation: CAA47707.1. AL355932 Genomic DNA. Translation: CAB91426.1. AABX02000005 Genomic DNA. Translation: EAA27730.1.
PIR	S36364.
RefSeq	XP_956966.1. XM_951873.2.
UniGene	Ncr.420.
3D structure databases
ProteinModelPortal	P14804.
SMR	P14804. Positions 36-626.
ModBase	Search...
Protein-protein interaction databases
STRING	5141.NCU01517.1.
Protein family/group databases
Allergome	10750. Neu cr Glucoamylase.
CAZy	CBM20. Carbohydrate-Binding Module Family 20. GH15. Glycoside Hydrolase Family 15.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000001634; EFNCRP00000001634; EFNCRG00000001632.
GeneID	3873129.
KEGG	ncr:NCU01517.
Phylogenomic databases
eggNOG	COG3387.
HOGENOM	HOG000182646.
KO	K01178.
OrthoDB	EOG4FFH90.
Family and domain databases
Gene3D	1.50.10.10. 1 hit. 2.60.40.10. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR013784. Carb-bd-like_fold. IPR002044. CBM_fam20. IPR000165. Glucoamylase. IPR008291. Glucoamylase_SBD. IPR015902. Glyco_hydro_13. IPR011613. Glyco_hydro_15. IPR013783. Ig-like_fold. [Graphical view]
PANTHER	PTHR10357. PTHR10357. 1 hit.
Pfam	PF00686. CBM_20. 1 hit. PF00723. Glyco_hydro_15. 1 hit. [Graphical view]
PIRSF	PIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTS	PR00736. GLHYDRLASE15.
SMART	SM01065. CBM_2. 1 hit. [Graphical view]
SUPFAM	SSF49452. CBD_4. 1 hit. SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS51166. CBM20. 1 hit. PS00820. GLUCOAMYLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMYG_NEUCR

Accession

Primary (citable) accession number: P14804
Secondary accession number(s): Q7RV62, Q9P5U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 30, 2003
Last modified:	April 3, 2013
This is version 118 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program