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Database: UniProt
Entry: A0A0M2PE65_9BACI
LinkDB: A0A0M2PE65_9BACI
Original site: A0A0M2PE65_9BACI 
ID   A0A0M2PE65_9BACI        Unreviewed;       740 AA.
AC   A0A0M2PE65;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Glycosyl hydrolase family 65 {ECO:0000313|EMBL:KKI89053.1};
GN   ORFNames=WQ54_27890 {ECO:0000313|EMBL:KKI89053.1};
OS   Bacillus sp. SA1-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI89053.1, ECO:0000313|Proteomes:UP000034887};
RN   [1] {ECO:0000313|EMBL:KKI89053.1, ECO:0000313|Proteomes:UP000034887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1-12 {ECO:0000313|EMBL:KKI89053.1,
RC   ECO:0000313|Proteomes:UP000034887};
RA   Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT   nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC       {ECO:0000256|ARBA:ARBA00006768}.
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:KKI89053.1}.
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DR   EMBL; LATZ01000131; KKI89053.1; -; Genomic_DNA.
DR   RefSeq; WP_046589530.1; NZ_LATZ01000131.1.
DR   AlphaFoldDB; A0A0M2PE65; -.
DR   PATRIC; fig|1455638.3.peg.6180; -.
DR   OrthoDB; 9758855at2; -.
DR   Proteomes; UP000034887; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KKI89053.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..242
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          297..659
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   DOMAIN          669..730
FT                   /note="Glycoside hydrolase family 65 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03633"
FT   ACT_SITE        472
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT   BINDING         332..333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT   BINDING         572..573
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ   SEQUENCE   740 AA;  84105 MW;  DA33BC86F750F8DB CRC64;
     MKKKRGIYEH GFDLHYLNKY ASLLALGNGY LGIRGTHEED YTGQNRGMYV AGVYNKATAN
     EPSEIVNLPD ISGMVIEIDG QPFSLLQGEV VSYERVLHFE TGELRREIVW RSKAGARYQL
     LFQRFVSKHD LHVAALKVTI ISLDKQAEIK IVTGIDAQQT NFGKQHVIEE SVRVYNEEII
     QGVYQTTESG VIVAIAAGIH VPETSKVTFS AKNRQLLSGI SCKVAQAEPF VLEKIGTVYT
     SHECDDPETI SLEAVQTLTP KGYDGLLAQS AAMWQEFWQL KRVSITSSNE FDQTAMDFAL
     YHIEIMTPAH DERFSIGAKG LTGEGYKGHV FWDTEIFLAP FHLYTEPETA KKLLQYRYKH
     LQEAKEKAAQ NKYEGALFPW ESAFTGKEET PEFAAINIRT GTRQKVASAL AEHHIVADIA
     FAVVQYYEST IDEDFMKNEG LALLKETARF WISRTVDEGG KLSIHDVIGP DEYTEHINNN
     AYTNYLAYYN VEQALYFMEQ YMDEEAELFE KGRDFLKRLY LPEPNDEQII PQDDTFLTKS
     EIDLSPYKQK QGSQAILLDY SRKEVNEMQI LKQADVVMLL YLLPDLFSSE IVRKNLFYYE
     EHTIHDSSLS KAIHAIVAAR CDDYAAAYRF FQEACLIDLG TNPRSSDEGI HAASLGAIWL
     AAIFGFANMT MRADRLALTP KLPANWKELK FPLSYQGRKL EFKLTHQICE ITKLSGLELK
     IEINGSLFEL KDRLEVEITD
//
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