ID A0A0S2JJX6_9GAMM Unreviewed; 1072 AA.
AC A0A0S2JJX6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN ORFNames=CMT41_17145 {ECO:0000313|EMBL:ALO36264.1};
OS Colwellia sp. MT41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO36264.1, ECO:0000313|Proteomes:UP000065319};
RN [1] {ECO:0000313|EMBL:ALO36264.1, ECO:0000313|Proteomes:UP000065319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT41 {ECO:0000313|EMBL:ALO36264.1,
RC ECO:0000313|Proteomes:UP000065319};
RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA Yayanos A., Methe B.A., Bartlett D.H.;
RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT Colwellia.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP013145; ALO36264.1; -; Genomic_DNA.
DR RefSeq; WP_058027950.1; NZ_CP013145.1.
DR AlphaFoldDB; A0A0S2JJX6; -.
DR STRING; 58049.CMT41_17145; -.
DR KEGG; com:CMT41_17145; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000065319; Chromosome.
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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000065319};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1072
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006600339"
FT DOMAIN 763..1054
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1072 AA; 121216 MW; 371C77B302D013FD CRC64;
MKASLLFVIL GITFLTSSVL AKQALEPWQD HQVFAINKLA PHASFFPFST VNAALDDNKE
QSDNFILLNG LWQFDWQRSP KNKPQGFEQK GFDDANWSQI PVPGNWEVEG FGYPIYLDER
FPFSTTWPDV PKEYNPIGSY RKPFTLPKSW QNKQVILHIG AAKSSLDVWL NGKKVGFSQG
SKTPAEFDLT PYLDEGENVL ALQIRRWTDA SYLESQDMLR ISGIERDVYL YVQEQQHIVD
FYAKPKLSKN FSQAEFSVTV DVNNLAKSNS GKLTVAYQLL DPSNHLKSVI SAEKIITINS
EGKQQVSLSG SFAKPRLWNA ETPNLYTLLI TLTDENGRVL TAIKDDIGFR HIEIINSQLT
VNGKAIYIRG VDRHETSPKH GHVVTKALME QDIKLMKQFN INAVRSSHYP NDPYWYDLTD
KYGLYVIDEA NIESHPLAIN EKTQLGNEMS WLPAHLDRTK RMFERDKNHP SIIIWSLGNE
AGVGKIFSAT YKWLKEHDDS RLVQYEPAGE EHYTDIFSPM YPSIERLEKY AKSKPHRPAI
MIEYAHAMGN SVGNLQDYWD VIEKYDVLQG GFIWDWVDQS LEYTNSNGVK YWAYGKDFHP
YLPSDGNFLN NGLVNPNREP HPHLFEVKKV YQPVKFTAED LTKASFTITN KFAFSNLNQY
DLQWSLTADG ELVAQGQRAM ADIAAGKTKV MTLKKVLAHL PMSSNKEYFL TVKMVVNKPQ
PLLDSGHEVA FEQFKMPVKY QATKVQLGAD KTLERIDANG QLTLFNDNVA VAFSQKTGWL
TKFTYQGKSL ISPLVKQPLK VNFWRAPTDN DLGNGLQKRA KIWQQAAHSL QLVKLSSMTE
NASILVKAIY SSDLFVGSYQ VNYQISANGR IHVSSKLNLA DEQELADIPR MGMQLVMPGE
FQFISWFGRG PHENYADRKT SAAIGLYQAA VKEQIHHYAR PQENANKTDV RWLAMISPTG
AGLLAVGDKP LSVSAWPYLQ QDIDFVDGRD GSASASGLVP VTSKHGAELI MRDLVTVNID
DKQMGVGGDT SWGRLVHAAY RIPAKSYQYG FTLVPFIDEN DLAKLARSVE KK
//
