ID A0A0S8E9N7_9BACT Unreviewed; 864 AA.
AC A0A0S8E9N7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE Flags: Fragment;
GN ORFNames=AMJ65_01120 {ECO:0000313|EMBL:KPK45040.1};
OS Phycisphaerae bacterium SG8_4.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703409 {ECO:0000313|EMBL:KPK45040.1, ECO:0000313|Proteomes:UP000051853};
RN [1] {ECO:0000313|EMBL:KPK45040.1, ECO:0000313|Proteomes:UP000051853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_4 {ECO:0000313|EMBL:KPK45040.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
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:KPK45040.1}.
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DR EMBL; LJTR01000010; KPK45040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8E9N7; -.
DR Proteomes; UP000051853; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
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 InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..864
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006644984"
FT DOMAIN 51..185
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 202..288
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 296..369
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 559..650
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|Pfam:PF16353"
FT NON_TER 864
FT /evidence="ECO:0000313|EMBL:KPK45040.1"
SQ SEQUENCE 864 AA; 98792 MW; 31A9CD2DE68419F4 CRC64;
MPKLWMLTTV LLAFALGGNT LPAQETELQY LSGHGKDDPV KWQFHCSGGQ NSGRWTTIDV
PSNWEFQGFG TYNYGHDDPK ASEQGRYRYS FEMPRRWRDK TIFIVFEGVM TDTAAWINGK
SAGPEHQGGF YRFKYDITKL VKFNGGNLLE VTVDKVSSNA SVEAAERKAD YWVFGGIYRP
VYLEAFPQQF IERTAIDARA DGTISADVYL KNIVDVDQIV GTVTKRGVGE REVLSAELTA
GQSKVTLRGK VSGIESWTAE TPHLYDLELA LMKESTIIHR TAERFGFRTF EVRPGQGLFL
NGKKIRLKGV NRHCFWPDSG RCLSRQVSYD DVRLIKQMNM NAVRMSHYPP DKHFLEACDE
LGLYVLDELA GWQRPPYDTD IGKKLVRELV TRDVSHPCIL FWDNANEGGW NRQLDDQFAL
YDPQKRIVLH PWENFNGIDT DHYEGYESVR KKLSSSTLFM PTEFLHGLYD GGHGAGLNDY
WNLIQNSPLG AGGFLWALVD EGVVRTDKNG AIDTDGNHAP DGILGPYRQK EASFYTIKEI
WSPIQIGLRE LPDDFSGRIE VENRYGFTDL QDCQLEWRLA RFPRPFEDKD EHTVVDEGKL
RGPGVRPGDR GVLELELPDD WRQAHALYLK ASDPAGEDIW TWSWALKQDC GTCHQYVDQQ
SKKDAKISVT EKDRELLVKV DDLSLSFDKV TGQLAKVEKY GAHISFGAGP RLVTGDSRLA
DFKHYRDGND VYVETAYDNG LYAKWKVYPS GWMRLDYQYE LEGQFDLMGI TFDYPESKMR
KMRWVGRGPY RVWKNRTKGG RLDVWSNDYK DHTPGVTWDF PEFRGYYNGW QWAAFETEEG
KVTLLNGTED VFLGVYMPKN GPDP
//
