ID K6ZKU4_9ALTE Unreviewed; 1050 AA.
AC K6ZKU4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=C427_1910 {ECO:0000313|EMBL:AGH44019.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH44019.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH44019.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH44019.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
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}.
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DR EMBL; CP003837; AGH44019.1; -; Genomic_DNA.
DR RefSeq; WP_007636106.1; NZ_BAES01000022.1.
DR AlphaFoldDB; K6ZKU4; -.
DR STRING; 1129794.C427_1910; -.
DR KEGG; gps:C427_1910; -.
DR PATRIC; fig|1129794.4.peg.1891; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000011864; 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; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000011864};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1050
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003898393"
FT DOMAIN 766..1046
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1050 AA; 120167 MW; 003E1FAB58BB6C47 CRC64;
MKKYFSVWLA FTTSMFAQAV SAQSLDWQNP EVFRINKEPA RSFFYSYDNA QAAFSKTPWD
QANHILLNGQ WKFNWVDSVK KKPNDFYQTN FDDSQWGQIA VPANWEVNGY GTPFYHSHQC
FKANVVPPEM PAHYNPVGSY RKTFNLPDDW NEKQVFVHFG AVKSAFYLWV NGQKVGYSQD
SKTAAEFDIS TYLQVGENQL ALQVYRYSDG SYFECQDMWR VSGIERDVYL FATPKLHIKD
FHAYTTLTDN YSKGELQLSA LIDNNLNRTV SGYQLKLQLF DHQQKILFEK NLNIEKLSEN
KVAVIKYITS IDTPNLWSAE APYLYDLKLT LLDSQGKDIE HIGHNIGFRS TELKNGNILI
NGEPVLFKGV NRHEHDPVTA HVVTRELMLK DVQLMKQFNI NAVRMAHYPN DPYMYYLADL
YGLYVMDEAN TESHGVGAAN QGPYNPDTHL VNKPEWAAAY IDRVSNMYHA TKNNPSVVMR
SLGNESGDGP NLEATYDWLK QQEPNSPVIS EQAQMRRHTD AYGQMYAPIS DIERYAKRKF
DTTRPVILIE YEHAMGNSLG NFKEYWDNFE KYPSLQGGFI WDWVDQTFAM KTLDGTPYWG
YGGDLEPDAT VSSLSFSANG LVFADRTPYP YLWEVKNVQQ NIGFSSDDIE TGVLNVINKN
YFVNLQGQSL SWQLLAEGNQ VAQGQGLPLS AKPQKSQQLQ LDYGIQRQPG VEYFLDVQVT
SDKTNGVIHQ GHITAWSQLA LPIVSIPADK QPEVRLAVSD KKQAYRFKGQ DFSLSIDKTT
GLISSMEYFG DELLKASPRP DFWRAPTDND LPIKDYGDKI APWQKAGKDT ALVSIKLTKE
SNYQAKVEVE HYISAIESRY FTTYHVFGNG KVKVEVYFYA APHKKQSDIP RLGTLFELDK
QYSQVTWYGR GPHENYMDRK TSAHVGQYQS NVADLYVPYV RPQENGYRSD VRNVSFHNQD
GKGITFKGAP LIGFGAQYYD TADYHATAAQ VKAKNIHPHE LPKKQRIFVN IDYMQRGVGG
TNTWGAEPLA DYIIPYLDYQ YSYSFEPYKQ
//
