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Database: UniProt
Entry: Q2B3F7_9BACI
LinkDB: Q2B3F7_9BACI
Original site: Q2B3F7_9BACI 
ID   Q2B3F7_9BACI            Unreviewed;       845 AA.
AC   Q2B3F7;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Alpha-glucosidase, family 31 of glycosyl hydrolase {ECO:0000313|EMBL:EAR64417.1};
GN   ORFNames=B14911_17785 {ECO:0000313|EMBL:EAR64417.1};
OS   Bacillus sp. NRRL B-14911.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=313627 {ECO:0000313|EMBL:EAR64417.1, ECO:0000313|Proteomes:UP000004554};
RN   [1] {ECO:0000313|EMBL:EAR64417.1, ECO:0000313|Proteomes:UP000004554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-14911 {ECO:0000313|EMBL:EAR64417.1,
RC   ECO:0000313|Proteomes:UP000004554};
RA   Siefert J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAR64417.1}.
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DR   EMBL; AAOX01000025; EAR64417.1; -; Genomic_DNA.
DR   RefSeq; WP_009792246.1; NZ_CH672355.1.
DR   AlphaFoldDB; Q2B3F7; -.
DR   GeneID; 85550713; -.
DR   HOGENOM; CLU_000631_7_2_9; -.
DR   Proteomes; UP000004554; Unassembled WGS sequence.
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; cd06604; GH31_glucosidase_II_MalA; 1.
DR   CDD; cd14752; GH31_N; 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; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF166; ALPHA-GLUCOSIDASE; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 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; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:EAR64417.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..845
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004206130"
FT   DOMAIN          72..237
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          281..610
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          619..706
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          722..789
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
SQ   SEQUENCE   845 AA;  96787 MW;  7566F756B0B1F3D4 CRC64;
     MAKSRKTLRM LAAAAIAAGV ALSASIPGAL AVTQPEADTP LKKENLQTLS AKSVKKLKNG
     VQFDLGDYEA FIRIYSEDLV KVSVLKDGQK EEETPAIAKK DWKTPLFSTE DGKKEYTIKT
     GELTIKVSKS PFGVKFLDKE GQVINEDYLQ NGASSGYEDG KPYVFKKTEK GENFYGFGEQ
     AGLNMNQRGE SIGMWNTDAY AYTKDTKYVY TSIPFFMGLK DKKAYGILFD NSYRSYYEMA
     SESDDYYYFY ANGGPLTYYF MYGPEISDVL DRYTELTGKM DMPAEWTLGL HQSKWGYTAD
     EITDVAQTYR DKNIPLDTMH FDIDYMQGYR VFTWDQKYKD ALSKLKSMEG FHAIAINDPA
     VKQDENYKIY QEGTAKDFWG KNPDGTNFIG PVWPGDSAFP DFSKEEVRDW WAKNHNVLFD
     AGIDGIWNDM NEPAVFVDGG EYNHTMPLDT YFGYEDDKIM HTEYHNLYGH DEAEATYNAW
     AMHKPNERPF VLTRDMFAGS QRYAALWTGD NESNWEHLQM SLPMNMNLGL SGVSFVGNDI
     GGFASRPDKE LYTRWIEVGA FLPFSRIHYD SDAKAEVKQG QEPWAFGPEV EGIAKKYIEM
     RYQLMPYLYN AFKDSSETGK PVQQPLVYHY QEDANTYDIA DQFMFGDSMM LAPVVKEGQT
     RRDVYLPKGD TWVDFWTKKE YKGGQTINVS APLEHLPIFV KKDSIIPTRE VQQYTGEKEL
     TNLVLDTYLD KEASYSFYED DGKSLDHQDG EFDITNFTLN EKPNKIEFTQ KKETDNYDST
     LQQVTLKLNN EKAPKRIQAA GKKYRAVFSL EEMTQTKESY FYETNSKTLY VNVPAAEGKK
     VQIKF
//
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