EXGD_EMENI
ID EXGD_EMENI Reviewed; 831 AA.
AC Q5AVZ7; C8VBL9; Q1HFR4;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Glucan 1,3-beta-glucosidase D;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase D;
GN Name=exgD; ORFNames=AN7533;
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: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan. {ECO:0000269|PubMed:16844780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; DQ490510; ABF50886.1; -; mRNA.
DR EMBL; AACD01000129; EAA62113.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF79583.1; -; Genomic_DNA.
DR RefSeq; XP_680802.1; XM_675710.1.
DR AlphaFoldDB; Q5AVZ7; -.
DR SMR; Q5AVZ7; -.
DR STRING; 162425.CADANIAP00000639; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EXG5D_EMENI; -.
DR PRIDE; Q5AVZ7; -.
DR EnsemblFungi; CBF79583; CBF79583; ANIA_07533.
DR EnsemblFungi; EAA62113; EAA62113; AN7533.2.
DR GeneID; 2869497; -.
DR KEGG; ani:AN7533.2; -.
DR VEuPathDB; FungiDB:AN7533; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_4_0_1; -.
DR InParanoid; Q5AVZ7; -.
DR OMA; THQYTIF; -.
DR OrthoDB; 896412at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell membrane; Cell wall biogenesis/degradation;
KW Glycoprotein; Glycosidase; Hydrolase; Membrane; Polysaccharide degradation;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..831
FT /note="Glucan 1,3-beta-glucosidase D"
FT /id="PRO_0000395168"
FT TOPO_DOM 1..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 322..831
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 598
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 703
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 831 AA; 95363 MW; 9A08532CA04B7B3E CRC64;
MPSQSRSRDR YGRDSDRDRS RVQPRRRYHV SEDDDDDDDF DDNPRDRRYR RDGYRRAPVD
SRAYDSHDDY EVVDVEEEPR RYRSDTERRR ERARASPGTS PRKRERTRDS GGGHRRRRTE
ESDGSQAPQA HRDRRSRTRR DRGLDDEDLE DAARRLRRRE RERERERRAE TSKHKSTDSS
NSSAGLLNAN ALAKLRAQHE ELDRQEQRRA EKEAKAERKR RRKRPAVEGQ MRTLDPFPDE
VPRGQSKGRI VSGAYLEEGR APDMEVRLRG GGRGPPRERR WEKDSDGSAP LTPFWKRKKW
WWIGAIVLVI VVIIIVVAVV VSNNKKSDSD SDSDSNSGSS DSWGGDKSSL NGLDHDSIPK
SAQGTVLDPW TWYETTDFNV TYTDETVGGL SVMGLNSTWD DSVAPNENVP PLNKPFPYGS
QPIRGVNIGG LLSLEPFITP SLFEGYSSDV VDEYTLTTKL GDNAARKLEE HYATFITEQD
FADMAEAGID HVRIPFSYWA VNPREDEPYV AKISWRYLLR VIEYCRKYGL RVNLDPHGMP
GSQNGMNHSG RQGSIRWLNG DDGDTYAQRS LEFHEKISKF FAQDRYKNII TIYGLINEPY
MLSLDVEKVL NWTVTAAELV QKNGITAKIA FHDGFLNLSK WKTMLKNGPS NLLLDTHQYT
IYNVAQIVLN HTAKVNFVCN DWVGMIGEIN STSEGWGPTI CGEFTQADTD CAKNLNNVGR
GTRWEGTYSE GDSTMYCPTA EQRTCSCTEA NADPSEYSDD YKLFLKTYAE AQMYAFEQAQ
GWFYWTWHTE SAPQWSYKTG WKNGFMPAKA YNPDYKCGDD IPSFGNLPEY Y
