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Database: UniProt
Entry: A0A0D6A155_9LACO
LinkDB: A0A0D6A155_9LACO
Original site: A0A0D6A155_9LACO 
ID   A0A0D6A155_9LACO        Unreviewed;      1003 AA.
AC   A0A0D6A155;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:BAQ56552.1};
GN   ORFNames=LBAT_0163 {ECO:0000313|EMBL:BAQ56552.1};
OS   Lactobacillus acetotolerans.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1600 {ECO:0000313|EMBL:BAQ56552.1, ECO:0000313|Proteomes:UP000035709};
RN   [1] {ECO:0000313|EMBL:BAQ56552.1, ECO:0000313|Proteomes:UP000035709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13120 {ECO:0000313|EMBL:BAQ56552.1,
RC   ECO:0000313|Proteomes:UP000035709};
RA   Toh H., Morita H., Fujita N.;
RT   "Complete genome sequence of Lactobacillus acetotolerans NBRC 13120.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; AP014808; BAQ56552.1; -; Genomic_DNA.
DR   RefSeq; WP_060459088.1; NZ_AP014808.1.
DR   AlphaFoldDB; A0A0D6A155; -.
DR   STRING; 1600.LBAT_0163; -.
DR   KEGG; lae:LBAT_0163; -.
DR   PATRIC; fig|1600.4.peg.167; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000035709; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF54; BCDNA.GH04962; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035709}.
FT   DOMAIN          273..509
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          516..612
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          620..684
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
FT   DOMAIN          875..991
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
SQ   SEQUENCE   1003 AA;  114216 MW;  B48A1686150EFEBC CRC64;
     MTQDTQMNKH QLGQLIGANR RDHYYELHYA TGEVARFYIL GDGIFHYFLD PDKSFNENHT
     SFVDLSRFDN HFFEKSSARA TSDSLIIQSG IYQIIFQQKP ALMSIFDENL HRTRMTQIAP
     IELDKDQTTE FLKQNKNEFY FGGGMQNGYF SHKGRRINIK RDKITGKDGV LTQVPFFWSN
     AGFGELRNTV RAGSYDFGKS DKSVTALTHT SKVFDNFYII GNSPTVILDK YYLLTGKPLM
     LPKYALGLGH IGNFITTMWQ PSQAKKRNAS RFDNNSYYTR TNDPKKVSGK ASLNGEEEYQ
     FSARAMIDRY QKLHFPLSWF VPNYGVQDVD QDSLATFNDY ANNQDTHAGF WSNQAVTEPS
     PKTAFIMTNT SFSKVLDKDQ QSLKTNLKRK RPLILTNTGT AGSQNKTALA FGDTGGNWEN
     IPTQIASFLG SSLSGQPIVG AAIDGTNGGG NAQISIRDFE WKAFTPLFFN IDDQGTFSKT
     PFAYNSKMTQ INRAYLQLRN QLKNYLYTLI YKAQTGDPIL RALFIEFPHE QVNYTSQVGN
     EFMLGPNLLI SPITNGREDS NGNSRKDNLY LPSHRTMWID LFTGKRYLGG RVFNKLSYPL
     WHLPVFIRGG AIFDLGNRNY ILYPQGRSEI TTYDDNDFND FNHNHTETKI TSDFESSRLT
     VTIDPVKGDF NGMKTNNSTN LNIMCDSYPD RVTVRINDQT INMQEYGTPD TFSHAKEGFF
     YNTDYTWLPE FNQYQKEKQT ALQIKLASRD ITDSKIEVII QNFNYGNQTL VHSITDSLLR
     APKLPTVDPT KITAHSFELA WPQVSNQVQV EINGLLYDGI DGTSFTFHEL TPNSRYIIRL
     RYVAGNKVSE WSDYFGVITK RAAIDYAINN IHVQSNLDSN KDHPLNYLTD LKLASEWETN
     ESVSEDKPLQ LTFTFDELEK LSRMTYVPRN VDHKGDPTSV GIEISSDGEK FASYGDRLTW
     KADSKNKVVG LRDVTAKAIR LTIYKSSGPI VAGREVMFFR AKK
//
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