ID C0MF95_STRS7 Unreviewed; 539 AA.
AC C0MF95;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Glucan 1,6-alpha-glucosidase {ECO:0000313|EMBL:CAW97914.1};
GN OrderedLocusNames=SZO_01960 {ECO:0000313|EMBL:CAW97914.1};
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN [1] {ECO:0000313|EMBL:CAW97914.1, ECO:0000313|Proteomes:UP000001368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70 {ECO:0000313|EMBL:CAW97914.1,
RC ECO:0000313|Proteomes:UP000001368};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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DR EMBL; FM204884; CAW97914.1; -; Genomic_DNA.
DR AlphaFoldDB; C0MF95; -.
DR KEGG; seq:SZO_01960; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_1_2_9; -.
DR Proteomes; UP000001368; Chromosome.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
FT DOMAIN 13..402
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 539 AA; 62155 MW; 8A4A6204516D5C0E CRC64;
MEKHWWHKAT IYQIYPRSFM DTSGNGIGDL KGITGKLDYL QELGITAIWL SPVYQSPMDD
NGYDISDYQA IAAIFGDMAD MDELLDEAKQ RGIKIIMDLV VNHTSDEHAW FVEARENPDS
PKRDYYIWRD QPNNLMSIFS GSAWEYDDAS GQYYLHLFSK KQPDLNWENA ELRQSIYDMM
NFWIDKGIGG FRMDVIDLIG KIPDSEITGN GPRLHEYLKE MNQASFGNHD LMTVGETWGA
TPEIARQYSR PENKELSMVF QFEHIGLQHK PNAPKWDYAA ELNVPALKEI FSKWQTELKL
GEGWNSLFWN NHDLPRVVSI WGNDTVYREK SAKAMAILLH LMRGTPYIYQ GEEIGMTNYP
FERLSDVNDI ESLNYAKEAM ANGMSEEAVL DSICRVGRDN ARTPMQWSSQ KNAGFSTADQ
TWLPVNPNHQ EINVASALAD PDSVFYTYQK LIQLRQTQDW LVEADYQLLQ TSDKVFAYKR
QLGRETYLVV VNLSNQEQFF EESLHKVQVI ISNTDVQAVV ESQQLEPWDA FCVKLDETL
//