BTGC_EMENI
ID BTGC_EMENI Reviewed; 649 AA.
AC Q5B430; C8VAX6; Q1HFT1;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase btgC;
DE EC=3.2.1.39;
DE AltName: Full=Endo-1,3-beta-glucanase btgC;
DE AltName: Full=Laminarinase btgC;
GN Name=btgC; ORFNames=AN4700;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT "Development and application of a suite of polysaccharide-degrading enzymes
RT for analyzing plant cell walls.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: Glucanases play a role in cell expansion during growth, in
CC cell-cell fusion during mating, and in spore release during
CC sporulation. This enzyme may be involved in beta-glucan degradation.
CC Active on laminarin and lichenan. {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; DQ490493; ABF50869.1; -; mRNA.
DR EMBL; AACD01000080; EAA60742.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF76969.1; -; Genomic_DNA.
DR RefSeq; XP_662304.1; XM_657212.1.
DR AlphaFoldDB; Q5B430; -.
DR SMR; Q5B430; -.
DR STRING; 227321.Q5B430; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR CLAE; LAM17A_EMENI; -.
DR PRIDE; Q5B430; -.
DR EnsemblFungi; CBF76969; CBF76969; ANIA_04700.
DR EnsemblFungi; EAA60742; EAA60742; AN4700.2.
DR GeneID; 2872500; -.
DR KEGG; ani:AN4700.2; -.
DR VEuPathDB; FungiDB:AN4700; -.
DR eggNOG; ENOG502QTKT; Eukaryota.
DR HOGENOM; CLU_011476_0_1_1; -.
DR InParanoid; Q5B430; -.
DR OMA; PLNTQYP; -.
DR OrthoDB; 1163530at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell membrane; Cell wall biogenesis/degradation;
KW Glycoprotein; Hydrolase; Membrane; Polysaccharide degradation;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..649
FT /note="Glucan endo-1,3-beta-glucosidase btgC"
FT /id="PRO_0000395128"
FT TOPO_DOM 1..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 551
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 649 AA; 68963 MW; 8476F1DF5B3F1D93 CRC64;
MGDRSEQYGD IPPISSQHRM HGYGNNGEPA AMPGDGQQNW GSGPGIAHTH SMRTASTATP
GMDNLGPSAV GGGISGIALG VANTHDRQSG IDAFRDADAT LGYIPAERGY HTTGADNPYV
PSPPSVGPGP DESSEGLRSH ETFGSSAALS AAGAPAGNWT PPSGSRHSFL DGSYQGVASG
PYQRHSAYSS QDYPADINPD DILDDGDDGF AAAPSNKPNA AGGAATGGAA GGLLGEFFGA
KKAADASYDP VPGAGLPSVE KYAKPRPSGA SRKRGWIIGG ILAFIVIGAI VGGAVGGTLG
NRRSETASES SEVSADDDTE TNGDLDKNSD EIKSLMAMEG LHKVFPGMDY TPWGVQHPEC
DKWPPSQNNV TRDMAVLSRL TNTVRLYGTD CNQTEMVLHA IDRLELTDMK LWLGVWIDTN
TTTNERQLSQ LYDILDKRSD HSVFKGAIIG NEALYRAGST KEEARKNIID YMRQVRKHFN
DHNIDIKVAT SDLGDNWDET LADATDVVMS NVHPFFGGVE VSKAAGWTWS FWNSHNAPLT
QGTNKGNIIA EVGWPSGGGN DCGDGANCKD DTSGAVAGVK QMNQFMADWV CPALENGTDY
FWFEAFDEPW KVKFNKGDEQ WEDKWGLMDP GRNLKPGIEI PDCGGKTAA
