ID A0A1G0QMY4_9BACT Unreviewed; 1057 AA.
AC A0A1G0QMY4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=A2080_01240 {ECO:0000313|EMBL:OGU49184.1};
OS Ignavibacteria bacterium GWC2_36_12.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1798427 {ECO:0000313|EMBL:OGU49184.1, ECO:0000313|Proteomes:UP000178676};
RN [1] {ECO:0000313|EMBL:OGU49184.1, ECO:0000313|Proteomes:UP000178676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGU49184.1}.
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DR EMBL; MGZZ01000156; OGU49184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0QMY4; -.
DR STRING; 1798427.A2080_01240; -.
DR Proteomes; UP000178676; 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; 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 SMART; SM01038; Bgal_small_N; 1.
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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 763..1035
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1057 AA; 120349 MW; 4F84F4475B4449E9 CRC64;
MLLIGIQELS FAQNSLGTLP DWQNPLVIGI NKEPAHLSFM HYPDLLSALA DSGLEVHTPY
YKSLDGQWKF KWSKNPAERP KDFYKTDYDV SNWANIRVPA SWQTEGFGTA IYLNEKYPFH
PEYPVNPPLI PDDYNPIGSY RTTFAVPNNW DGRDVYIHFG AVESAFYIWV NGKKVGYSQG
SMTPAEFNLS SYLQKGENQL SVEVYRWSDG SYLEDQDMWR FAGIFRTVYL YSTPKVHLLD
FFIRAKLDDR YEDGLLHITA KVRNSSKENL KPAKVEAYLY DNNGKLPGNS LIVESETSSN
IPSGMLAVAD LYAKIDNPQK WTAETPNLYT VILVLKDDKG NVLEAARSTT GFRTVEIKDG
MLLVNGVPLK LKGTNIHDID PFHGRAVDYK WIEKDLKLMK QCNINAVRFS HYPHDPRYYD
IFDKYGMYVI DEANLETHGI SFRRDLLPGS DPLWTDACLE RMKRMIATNK NHPSVIIWSL
GNEAGHGENF SIMAAYARVV DPSRPIHYQH MNSIADMQSY MYPTPQQLES YANDPDITKP
IILCEYVHSM GNSTGNMEVY WDLIYNHKNI IGALIWDWVD QGLYKKDKNG KMFWAYGGDM
GDEVNDGNFC INGIVQPDRT PEPEYYETKH TYQFVNLIPM NLSEGSLIIR NGYYHSELSN
YELRWNLTEN GKVIQSGIID TLRTPAGSSS RIDLPIKQPE LVPGCEYWLN LSVHTKKKEF
WADKGFEVAW NQFKMPWAVA PAPMKDVSGM SNVQFEESEN SIVLNGEEFK ISINKKDGSL
VSYNWKGKDL ISGALQSNYW RAPTDNDAAG FKNDLDAWKN AGVGRKVENI NVAQPDKNIV
VVSAQGNLPV GKTTWQILYT VFGDGTVKVS QHLIPVGDVP YDIPKVGAEM RIPNEYNKMS
WYGRGPWDNY LDRLSGANVG IYSGLVDSLW TNYVRPQENG NRCDVRWIAF TNKNGEGLLA
VGDPTLSVSA WPYYLQDLEQ AKHINDLPHR DFITLNLDYK QMGVGGINTW NQHARPLPQF
CLPSSESYNY EFYLMPYSPD LGSMDDVARN NLPESNK
//
