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Database: UniProt
Entry: A0A1M3M8Y4_9BACT
LinkDB: A0A1M3M8Y4_9BACT
Original site: A0A1M3M8Y4_9BACT 
ID   A0A1M3M8Y4_9BACT        Unreviewed;      1017 AA.
AC   A0A1M3M8Y4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:OJX88035.1};
GN   ORFNames=BGP01_07030 {ECO:0000313|EMBL:OJX88035.1};
OS   Paludibacter sp. 47-17.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC   Paludibacter.
OX   NCBI_TaxID=1895899 {ECO:0000313|EMBL:OJX88035.1, ECO:0000313|Proteomes:UP000183960};
RN   [1] {ECO:0000313|EMBL:OJX88035.1, ECO:0000313|Proteomes:UP000183960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47-17 {ECO:0000313|EMBL:OJX88035.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:OJX88035.1}.
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DR   EMBL; MKVT01000023; OJX88035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3M8Y4; -.
DR   STRING; 1895899.BGP01_07030; -.
DR   Proteomes; UP000183960; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1017
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009895159"
FT   DOMAIN          72..196
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          221..320
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          655..709
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          726..825
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   1017 AA;  114199 MW;  211B351BBCE45981 CRC64;
     MHMKKNLVLL LMLTLLVQLG AAPVFKGNVR TKYNFNPQWK MHVGDDPGTS AAFSDPRFND
     SGWKQVDLPR AFNEDEAFQV AIDEHTDTII WYRKHFRLPR EARGQKIFLE FEGIRFGGEF
     WVNGKLVGGH DNGVMAFGLD ITEFVDYSGP NVVAARIDNS WRYRERATNS TFQWNDRNFN
     ANYGGIPKNV LLHVTPKVYQ TLPLFSNLGT TGTYIYAREI NISKKSAAVY AESEVKNESG
     SEQTVAFKVM IEDAEGKPVK TIEGPSKSLK AGETTVLKAG AVVENLHFWS WGYGYLYDVY
     TVLYVDGIAS DVVKTRTGFR KTAFRNGMVW INDRVLQMKG YAQRTSNEWP AVGMSVPAWL
     SDFSNNLIVE GNGNLVRWMH VTPWKQDVES CDRVGLIQAM PAGDAERDVT GRRWEQRVEL
     MRDAIIYNRN NPSIVFYESG NESISEDHMA EMVAVRDLYD PYGGRAMGSR EMLDSKIAEW
     GGEMLYINKS AKHPMWATEY LRDEALRKYW DESSYPWHKN GEGSKYYRST VSNELVQRPD
     ASAYNRNQNT FFVETIVRWY DYFRVRPGTG KRVSSGGANI IFSDSNTHFR GAENYRRSGE
     VDPMRIPKDA FYAHQVMWNG WVDIERHGTY ICGHWQQPAK APVAGAAPES LATRQVLVVS
     TGEKVELLVN GRSQGFGRRD YHFLYTFDDV KFEAGTVEAV SYDADGNELS RTKKETAGKP
     ERITLKLMQA PDGFKADGAD LVMVEIEVTD AAGRRCPLAN NAISFDLKGE AEWRGGIAQG
     KEGNFILDKI LPVEAGINRV LIRSTRKAGQ ISLTAKSEGL QPASLSFSSK PMKVKDGLSN
     YISGDCQPAR LSRGATPGSP SFTVKRVPVQ VVAATSGSGE DSVHLSWDDN ELTAWGNDGA
     MSSAWIRYEL ERDATLNEIE LKMSNWRNRS YPIRIYVDNE VVYEGATLQS LGYVALPLKP
     VKGRFVTIQL TGRNIEADAF GGIVEVTGQK EIETPAATAR GQLRIVEAEF YEQLKVD
//
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