Q5B430 (BTGC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucan endo-1,3-beta-glucosidase btgC
EC=3.2.1.39

Alternative name(s):
Endo-1,3-beta-glucanase btgC
Laminarinase btgC

Gene names

Name:	btgC
ORF Names:	AN4700

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	649 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation. Acive on laminarin and lichenan. Ref.1
Catalytic activity	Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Subcellular location	Cell membrane; Single-pass type II membrane protein By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation
Cellular component	Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	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	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glucan endo-1,3-beta-D-glucosidase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 649	649	Glucan endo-1,3-beta-glucosidase btgC		PRO_0000395128
Regions
	Topological domain	1 – 274	274	Cytoplasmic Potential
	Transmembrane	275 – 295	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	296 – 649	354	Extracellular Potential
	Compositional bias	222 – 300	79	Gly-rich
Sites
	Active site	551	1	Nucleophile By similarity
	Active site	619	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	369	1	N-linked (GlcNAc...) Potential
	Glycosylation	392	1	N-linked (GlcNAc...) Potential
	Glycosylation	420	1	N-linked (GlcNAc...) Potential
	Glycosylation	596	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5B430 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 8476F1DF5B3F1D93	FASTA	649	68,963
	10 20 30 40 50 60 MGDRSEQYGD IPPISSQHRM HGYGNNGEPA AMPGDGQQNW GSGPGIAHTH SMRTASTATP 70 80 90 100 110 120 GMDNLGPSAV GGGISGIALG VANTHDRQSG IDAFRDADAT LGYIPAERGY HTTGADNPYV 130 140 150 160 170 180 PSPPSVGPGP DESSEGLRSH ETFGSSAALS AAGAPAGNWT PPSGSRHSFL DGSYQGVASG 190 200 210 220 230 240 PYQRHSAYSS QDYPADINPD DILDDGDDGF AAAPSNKPNA AGGAATGGAA GGLLGEFFGA 250 260 270 280 290 300 KKAADASYDP VPGAGLPSVE KYAKPRPSGA SRKRGWIIGG ILAFIVIGAI VGGAVGGTLG 310 320 330 340 350 360 NRRSETASES SEVSADDDTE TNGDLDKNSD EIKSLMAMEG LHKVFPGMDY TPWGVQHPEC 370 380 390 400 410 420 DKWPPSQNNV TRDMAVLSRL TNTVRLYGTD CNQTEMVLHA IDRLELTDMK LWLGVWIDTN 430 440 450 460 470 480 TTTNERQLSQ LYDILDKRSD HSVFKGAIIG NEALYRAGST KEEARKNIID YMRQVRKHFN 490 500 510 520 530 540 DHNIDIKVAT SDLGDNWDET LADATDVVMS NVHPFFGGVE VSKAAGWTWS FWNSHNAPLT 550 560 570 580 590 600 QGTNKGNIIA EVGWPSGGGN DCGDGANCKD DTSGAVAGVK QMNQFMADWV CPALENGTDY 610 620 630 640 FWFEAFDEPW KVKFNKGDEQ WEDKWGLMDP GRNLKPGIEI PDCGGKTAA

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	DQ490493 mRNA. Translation: ABF50869.1. AACD01000080 Genomic DNA. Translation: EAA60742.1. BN001303 Genomic DNA. Translation: CBF76969.1.
RefSeq	XP_662304.1. XM_657212.1.
3D structure databases
ProteinModelPortal	Q5B430.
ModBase	Search...
Protein family/group databases
CAZy	GH17. Glycoside Hydrolase Family 17.
mycoCLAP	LAM17A_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00005730; CADANIAP00005730; CADANIAG00005730.
GeneID	2872500.
KEGG	ani:AN4700.2.
Phylogenomic databases
eggNOG	COG5309.
HOGENOM	HOG000173877.
OMA	TEMVLHA.
OrthoDB	EOG4KD9WH.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00587. GLYCOSYL_HYDROL_F17. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BTGC_EMENI

Accession

Primary (citable) accession number: Q5B430
Secondary accession number(s): C8VAX6, Q1HFT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program