ID C9SNA7_VERA1 Unreviewed; 583 AA.
AC C9SNA7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Glucoamylase {ECO:0000256|PIRNR:PIRNR001031};
DE EC=3.2.1.3 {ECO:0000256|PIRNR:PIRNR001031};
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|PIRNR:PIRNR001031};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|PIRNR:PIRNR001031};
GN ORFNames=VDBG_06382 {ECO:0000313|EMBL:EEY20272.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000256|ARBA:ARBA00001863,
CC ECO:0000256|PIRNR:PIRNR001031};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC {ECO:0000256|ARBA:ARBA00006188, ECO:0000256|PIRNR:PIRNR001031}.
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DR EMBL; DS985220; EEY20272.1; -; Genomic_DNA.
DR RefSeq; XP_003003939.1; XM_003003893.1.
DR AlphaFoldDB; C9SNA7; -.
DR STRING; 526221.C9SNA7; -.
DR GeneID; 9535533; -.
DR KEGG; val:VDBG_06382; -.
DR eggNOG; ENOG502QPM2; Eukaryota.
DR HOGENOM; CLU_012173_1_0_1; -.
DR OMA; NRKYTVP; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd05811; CBM20_glucoamylase; 1.
DR Gene3D; 1.50.10.10; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034836; CBM20_glucoamylase.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR InterPro; IPR046966; Glucoamylase_active_site.
DR InterPro; IPR008291; Glucoamylase_SBD.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR31616:SF12; GLUCOAMYLASE-RELATED; 1.
DR PANTHER; PTHR31616; TREHALASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF00723; Glyco_hydro_15; 2.
DR PIRSF; PIRSF001031; Glu-a-glcsd_SBD; 2.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00820; GLUCOAMYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR001031};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001031};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001031};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PIRNR:PIRNR001031};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..583
FT /note="Glucoamylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003002487"
FT DOMAIN 475..583
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT ACT_SITE 207
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-1"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001031-2"
SQ SEQUENCE 583 AA; 61797 MW; 7AD2F8B33E95EA81 CRC64;
MRFSSILSLG GLAVQSVSGL PGTLEKRVNV DQWIQQELPI ARAQLLCNIG PNGCNSAGVA
SGLVIASPSK SDPDYFFHWT RDAGLVFKAI IDLFVENYDA GLQQNIQNFI VGQAKLQTVN
NPSGSFSSGA GLGEAKYLAN GAQFTGDWGR PQRDGPALRA IALIKYSKWL IANGYTSTAN
TVVWPIIRND LAYVTQYWNQ TGFDLWEEVQ GSSFFTIASQ HRSLVEGAAL AQQLGQTCNG
CAGIAPQILC FQQRFWNPSQ GYVISNINGG SYRNGKDANS ILTSIHNFDP VLGCDASTFQ
PCSDRALSNH KVVTDSFRSI YGINNGKGQG QAALIPGIST GTYASTSSTY TSILSAVKAY
ADGYVDVAAT YIPGGGNIAE QYNRNTGQPL SARDLTWSYA SFLTVAQRRR EVVGLGWANS
AASVVPNTCF ATSVQGSYTS ATATSFPANQ TPATGAPTGT ATTATAPAAT TTAACVPPVN
VDITFNARVV TQFGQTVKIV GNIPQLGNWN TANAISLSAS QYTSSNPVWS GTLSLPAGQA
IQYKYINVAS NGAVTWEKDP NRSYSIPSAC GTTSAIRTDS WQA
//
