ID D7GH77_PROFC Unreviewed; 580 AA.
AC D7GH77;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Alpha-1,4-glucosidase {ECO:0000313|EMBL:CBL57888.1};
DE EC=3.2.1.20 {ECO:0000313|EMBL:CBL57888.1};
GN Name=aglA {ECO:0000313|EMBL:CBL57888.1};
GN OrderedLocusNames=PFREUD_23740 {ECO:0000313|EMBL:CBL57888.1};
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL57888.1, ECO:0000313|Proteomes:UP000000936};
RN [1] {ECO:0000313|EMBL:CBL57888.1, ECO:0000313|Proteomes:UP000000936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC {ECO:0000313|Proteomes:UP000000936};
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(2010).
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DR EMBL; FN806773; CBL57888.1; -; Genomic_DNA.
DR RefSeq; WP_013162201.1; NC_014215.1.
DR AlphaFoldDB; D7GH77; -.
DR STRING; 754252.PFREUD_23740; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; pfr:PFREUD_23740; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_3_11; -.
DR Proteomes; UP000000936; Chromosome.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR CDD; cd11332; AmyAc_OligoGlu_TS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:CBL57888.1};
KW Hydrolase {ECO:0000313|EMBL:CBL57888.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000936}.
FT DOMAIN 35..446
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 63398 MW; 02EB47702DD9ECAB CRC64;
MSTPATGSNG QLPHQHAGHT ADRTKAWWRD AVIYQIYPRS FADSDGDGMG DLGGVREHLG
DLEALGVDAV WLSPFFPSPQ ADAGYDVADY RDVDPLFGTL DDFDALLAGA HQRGLRVVID
LVPNHTSSKH VWFTAALAAA PGSRERNHYV FRDGRGEHGE LPPNNWPSQF GGPAWTRVDD
GTANPQWYLH LFDAGQPDLN WDNPEVIDEF QDILRFWLNR GVDGFRVDVA HGLVKQQGLP
DVTSGEHDAL SRLDDPRWDQ PGVHDIYRGW HRVLEGFGGD RMLVAEAWVA DATRRALYVR
PDEMQQAFNF GYLMAGWDTA SVRHAIDDAL GANDAVGATT TWVLSNHDVV RHASRLGYPV
PASDQGAPAP TWTNGIGPDD PKPDDELGLS RARAATLGML ALPGSAYLYQ GEELGLPEVT
DLAPEVRQDP EFLRTAGAVI GRDGARVPLP WDSGAPAFGF SPSGRSWLPQ PASFADYAAN
EQRGHPGSTL EMYRAAIDLR RTHRLGAGRV HWNEANPGVL DFTNGEVRVV MNMSRSPQPL
GDHVLGDQGT RDQALLLESS PGSVIDGQLQ PDRCVWLLVG
//
