ID A0A0S8ANJ2_9BACT Unreviewed; 835 AA.
AC A0A0S8ANJ2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
DE Flags: Fragment;
GN ORFNames=AMS20_15130 {ECO:0000313|EMBL:KPK00662.1};
OS Gemmatimonas sp. SG8_28.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703357 {ECO:0000313|EMBL:KPK00662.1, ECO:0000313|Proteomes:UP000051120};
RN [1] {ECO:0000313|EMBL:KPK00662.1, ECO:0000313|Proteomes:UP000051120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_28 {ECO:0000313|EMBL:KPK00662.1};
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 ECO:0000256|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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:KPK00662.1}.
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DR EMBL; LJNQ01000328; KPK00662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8ANJ2; -.
DR Proteomes; UP000051120; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
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; IPR004199; B-gal_small/dom_5.
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; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
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; PF02929; Bgal_small_N; 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.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT DOMAIN 55..224
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 226..341
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 343..627
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 638..727
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|Pfam:PF16353"
FT DOMAIN 755..815
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|Pfam:PF02929"
FT NON_TER 835
FT /evidence="ECO:0000313|EMBL:KPK00662.1"
SQ SEQUENCE 835 AA; 94003 MW; 825398D804055142 CRC64;
MTVLLAVRPA VAQEVAEWEN PAVFAINKEP PHATAFPFEN RALALRRDLH ASTYFQSLNG
RWKFHWVRKP ADRPAEFYLD GYDDRGWPEI PVPGSWEVNG FGIPIYLNQP YPFEANPPFI
RHDDNPVGSY RTHFTVPDHW QGRRVYLHFG AVESAMYVWV NGRQVGYSED SRLPAEFDVT
EYVRPGQNLL AVEVYRWSDG SYLEDQDFWR LSGIERDVYL VAAPEVHVRD FEIVAALDSA
FVDGVLDVRL EVENRGTGRA EQWGLLVDLV DGTGASVLPR GAIGRDLSVT GGGRANVGFR
ETVPAPRHWT AETPNLYTVL ITLTDASGAT VEVLGSRVGF RNVEIRGGQL LVNGVAVLLK
GTNRHEHDPV TGHVLSEATM RRDVELMKQF NLNAVRTSHY PNDPRWYDLA DEYGLYIVDE
ANVESHGMGY GLATTLGNAP AWKAAHLDRT IRMVERDKNH PSVIIWSLGN EAGNGANFYA
TYQWIKTRDP TRPVQYERAG LEWNTDIYVP MYPGIDYIIR YAEQQPARPL IMCEYAHAMG
NSVGNLTDYW DAIKRYPALQ GGFIWDWVDQ GLLTRNAQGK EIFGYGGDFG PRGTSSDGNF
LINGLVSPDR KPHPSLWEVK KVYQSIDVEP VALGRGAVAV TNAYQFRDLA NVRLVWSRLA
DGVPIDSGVV ETLDLRAGER KEITLPLPGT APIRDAEYHL TVSFRLKTAE GLVPAGHEIA
WEQFPLPVAV QLPIAEPVAQ APLTVEERDS VVVVSGDRFG VTFDVRNGEL LSYRYKGREL
IREPLRPNFW RAPNDNDFGG DWQHKLGMWK SAGDRWEFRY VQVERPAPDE VRVTV
//
