ID   A0A1G4S151_9CAUL        Unreviewed;       954 AA.
AC   A0A1G4S151;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:SCW62731.1};
GN   ORFNames=SAMN02927928_2323 {ECO:0000313|EMBL:SCW62731.1};
OS   Asticcacaulis taihuensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=260084 {ECO:0000313|EMBL:SCW62731.1, ECO:0000313|Proteomes:UP000199150};
RN   [1] {ECO:0000313|EMBL:SCW62731.1, ECO:0000313|Proteomes:UP000199150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3431 {ECO:0000313|EMBL:SCW62731.1,
RC   ECO:0000313|Proteomes:UP000199150};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FMTS01000003; SCW62731.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4S151; -.
DR   STRING; 260084.SAMN02927928_2323; -.
DR   OrthoDB; 7578670at2; -.
DR   Proteomes; UP000199150; 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; 1.
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; IPR048230; GalA-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
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   NCBIfam; NF041462; GalA; 1.
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; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..954
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011522694"
FT   DOMAIN          88..208
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          219..324
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          333..567
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          626..680
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          696..800
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   954 AA;  105258 MW;  F152E31F7A800C42 CRC64;
     MNRRELFKSA SALAVVGLLP QVAIAGTNGP DAADKGPRET LLLDKGWRFH DGDIAMPVLI
     THDQTYNAAK AGRALGAASP AYDDSDWTEV TLPHDFVSFQ PIENGTNVDQ GYRRRGIVWY
     RNHLKFSDAD RGKHIELQLD GIATFATIWF NGTLVARNWS GYNSTYIDLT PYVTYGDSDN
     ALVVRVDATA MEGWWYEGGG IYRDAWIVKR NPVHIVTDGV FAHPVKEGDE WKVPIEVTLN
     NSGTKDKTVQ IVCTLLDAEE RKISEGFIDL TVPKLGNAVG KASMPALSDP ELWSIETPYL
     YRVLTRVTEG AEVWDEVTTT CGFRTERFDA QTGFYLNDKP LKIKGVCLHQ DHAGVGCAVP
     EGVLDFRLRK LKELGANAIR FSHNAQNKAL MDACDRHGFL VMAENRNFNA STDYLEQLEW
     LVRRDRNHPS VFLWSVFNEE PMQGTEQGYE MVRRMSAVVK ALDTSRPVTA AMNDGLFTAL
     NVSDAVDVVG INYQQHQYDA FHAAHPDIPM FSSEDTSAFM TRGEYKTDAV KHIMASYDDD
     AAPWGETHRA AWKEISARPF VAGTFVWTGF DYHGEPTPHT WPTNSSFFGI MDLCGFEKTA
     FYIHQAQWID DRPVLGLVPH WNWQSGDKVR VMACANLDEV ELFVNGKSAG KQAVDRLNMN
     YWTVDYAPGF IEVRGYRGSK LVSKVRNETT GKAVALRLVK DRPTLIGDGR DAMPIRVEAI
     DAKGRVVPDA NHKVTFGGTA AIIGLGNGDP NCLEAEKGDT RSLFNGLAQV IIQAPEMAGN
     AAAVINLTAR AESLKPANIE IRLDAPKAAT PRQPTMLPMM VLDSWFRAPN ATAHPDPNQR
     AADTDMNSWA WFRPGELFGA AKTDGYSLVA ANYTPFASIQ KNGGRVVFTS ITGTCDIYLD
     GQAIGRKDDP APSAMTVAIP PFGGSRRLSV VFKLKAGEPF GFGGLIRIGG PEKT
//