Q5AWI5 (AGDC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha/beta-glucosidase agdC
EC=3.2.1.20
EC=3.2.1.21

Gene names

Name:	agdC
Synonyms:	agdD
ORF Names:	AN7345

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › Emericella nidulans › mitosporic Emericella nidulans

Protein attributes

Sequence length	894 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity. Ref.1
Catalytic activity	Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose. Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 31 family.
Sequence caution	The sequence EAA61716.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucan catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha-glucosidase activity Inferred from direct assay Ref.1. Source: UniProtKB beta-glucosidase activity Inferred from direct assay Ref.1. Source: UniProtKB carbohydrate binding Inferred from electronic annotation. Source: InterPro maltose alpha-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 894	873	Alpha/beta-glucosidase agdC		PRO_0000394919
Sites
	Active site	429	1	Nucleophile By similarity
	Active site	432	1	By similarity
	Active site	600	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	137	1	N-linked (GlcNAc...) Potential
	Glycosylation	178	1	N-linked (GlcNAc...) Potential
	Glycosylation	300	1	N-linked (GlcNAc...) Potential
	Glycosylation	402	1	N-linked (GlcNAc...) Potential
	Glycosylation	482	1	N-linked (GlcNAc...) Potential
	Glycosylation	483	1	N-linked (GlcNAc...) Potential
	Glycosylation	536	1	N-linked (GlcNAc...) Potential
	Glycosylation	601	1	N-linked (GlcNAc...) Potential
	Glycosylation	637	1	N-linked (GlcNAc...) Potential
	Glycosylation	802	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5AWI5 [UniParc]. Last modified June 15, 2010. Version 2. Checksum: 6AE3AD13A10C594D	FASTA	894	100,075
	10 20 30 40 50 60 MAGTLLSWTP LALALMARAL SQLPLTDCPG YRVINVEERP RGLTADLTLA GTPCNVYGVD 70 80 90 100 110 120 IENLRLETDY DTNQRLHVKI YDADENVYQV PDSVFPRPVV NDQACADENT PELRFSYAED 130 140 150 160 170 180 PFSFAVSRAS NDETLFNTTG HNLIFQSQYV NLRTSLPQNP NLYGLGEHSD PLRLNTINYT 190 200 210 220 230 240 RTLWNRDAYT IPAGTNLYGA HPMYIDHRGE AGTHGVFLLN SNGMDIKIDK NSDNIQFLEY 250 260 270 280 290 300 NILGGVLDFY FFAGPSPKDV SVQYAEVAGL PAMVPYWGLG FHQCRYGYRD IFEVAAVVHN 310 320 330 340 350 360 YSEARIPLET MWTDIDYMDH RKVFTLDRER FPLDTVRALV QYLHQRDQHY IVMVDPAVAH 370 380 390 400 410 420 SENGAFTRGL EKDVFMRKQD GTLYQGAVWP GATVFPDWFH PNTSDYWINE FALFFNAESG 430 440 450 460 470 480 VDIDALWIDM NEAANFCDWP CTDPVAYAEE NNLPPEPPAV RPNPSSLPGF PAEFQPVNSN 490 500 510 520 530 540 NNNSSRKRET QVVIAARQGF VKVGNDNGNG RRLGLQGREL IDPPYKIANA AGSLSNKTMN 550 560 570 580 590 600 TDIFHANGLA EYDTHNLYGT MMSSLSRDAM LYRRPEKRPL VITRSTFAGA GSYVGHWLGD 610 620 630 640 650 660 NASTWTKYRI SIAQMLAFAS IFQIPMVGSD ACGFTGNTTE ELCSRWATLA AFNPFFRNHN 670 680 690 700 710 720 EYGMVSQEFY RWNSVAEAAR KAISIRYSLL DYLYTEFHEQ TVTGEPFLLP LFFVYPNDPN 730 740 750 760 770 780 VVGIDSQFFY GDAILVSPVI EEGKTEVHAY FPGDLFYDWY TGLPLRGNGE VITLTDIGYT 790 800 810 820 830 840 DIPLHVRGGK IVPVRTGSAG MNTTTEVRKS GFRLVIAPGL DGRAAGRLYI DDGESLEQTA 850 860 870 880 890 MVDVVFTYED GRVSVDGVFT LQTDLRVEAV TVFGDNVVER TIDLPLSGPG GVEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls." Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R. Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[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 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ490507 mRNA. Translation: ABF50883.1. AACD01000128 Genomic DNA. Translation: EAA61716.1. Sequence problems. BN001304 Genomic DNA. Translation: CBF78576.1.
RefSeq	XP_680614.1. XM_675522.1.
3D structure databases
ProteinModelPortal	Q5AWI5.
ModBase	Search...
Protein family/group databases
CAZy	GH31. Glycoside Hydrolase Family 31.
mycoCLAP	AGL31C_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2869771.
KEGG	ani:AN7345.2.
Phylogenomic databases
eggNOG	COG1501.
HOGENOM	HOG000041175.
KO	K01187.
OMA	EGEFEIN.
OrthoDB	EOG4J40R4.
Family and domain databases
InterPro	IPR011013. Gal_mutarotase_SF_dom. IPR000322. Glyco_hydro_31. IPR025887. Glyco_hydro_31_N_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR22762. PTHR22762. 1 hit.
Pfam	PF13802. Gal_mutarotas_2. 1 hit. PF01055. Glyco_hydro_31. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00129. GLYCOSYL_HYDROL_F31_1. False negative. PS00707. GLYCOSYL_HYDROL_F31_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGDC_EMENI

Accession

Primary (citable) accession number: Q5AWI5
Secondary accession number(s): C8VCK6, Q1HFR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	June 15, 2010
Last modified:	April 3, 2013
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program