ID A0A0C9M801_9FUNG Unreviewed; 471 AA.
AC A0A0C9M801;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00012593};
DE EC=3.2.1.3 {ECO:0000256|ARBA:ARBA00012593};
GN ORFNames=MAM1_0035d02635 {ECO:0000313|EMBL:GAN03184.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN03184.1};
RN [1] {ECO:0000313|EMBL:GAN03184.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN03184.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001863};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC {ECO:0000256|ARBA:ARBA00006188}.
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DR EMBL; DF836324; GAN03184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9M801; -.
DR STRING; 91626.A0A0C9M801; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005976; P:polysaccharide metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR PANTHER; PTHR31616:SF11; GLUCOAMYLASE, INTRACELLULAR SPORULATION-SPECIFIC; 1.
DR PANTHER; PTHR31616; TREHALASE; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:GAN03184.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..471
FT /note="glucan 1,4-alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002199371"
FT DOMAIN 54..462
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
SQ SEQUENCE 471 AA; 52524 MW; 76021A2B18FE5CF6 CRC64;
MFTSYLLILL TTSLVYYYSS TGSDAVATDS PLDVWVAKQH ATSFKTIMTN INPPGTSRGF
FAASLSTYKP DYFYTWTRDA ALVARVISSI PETNLTVLTD YVDFQISTQM TPTVCDCLGE
PKFNTDGSGY TGSWGRPQND GPAERAIAFI AIANRWQLEG HDPTYITDTL VPAITRDLDY
VASVWQEACF DLWEEIEGVH FYTLMVMRRA LLDAVDFFDA HSDTPFRSDH NYKSTAYQIE
KRIESFWSSH QNYITSTQDV RNGVQKPSGL DVSILLAANL VSSRNDGFFT PGSDKVLATA
HALEEAFKSI YPLNQQLDEH LGTSIGRYPE DIYDGVGTSA GNPWFIATAA YTELYYLAIK
EWKQVGVVVN DINMPFLHRL LGCSVASSSV IGLRNTHYYA PGSIELGQLV HRATVAADKY
LATIQYHQAR NGSMSEQFDR YIGYMAGARD LTWSHAAFIS AAKAKSFHTV F
//