ID K6X776_9ALTE Unreviewed; 1052 AA.
AC K6X776;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 Name=bgaM {ECO:0000313|EMBL:GAC16459.1};
GN ORFNames=GLIP_3848 {ECO:0000313|EMBL:GAC16459.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC16459.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC16459.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC16459.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC16459.1}.
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DR EMBL; BAEN01000076; GAC16459.1; -; Genomic_DNA.
DR AlphaFoldDB; K6X776; -.
DR STRING; 1127673.GLIP_3848; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000006334; 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; 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:UP000006334};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1052
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003896426"
FT DOMAIN 768..1048
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1052 AA; 120108 MW; 2E90F965AE1FB9FE CRC64;
MSNYLRFLKY VAVAAGMIIP AHATTLEWQN PEVFRVNKEP ARSFFYSYDN PQAAFSKTPW
DQSNHLLLNG SWKFKWVESV TKKPSDFYKT EYDDSKWGEI TVPANWEVNG YGTPFYHSHQ
CFKANAVPPE MPSYYNPVGS YRKTFTVPDD WQQKQVFVHL GAVKSAFYIW VNGKKVGYSQ
DSKTAAEFDI SPYLKKGQNQ LALEVYRYSD GSYFECQDMW RVSGIERDVY LYATPKAHVK
DFHAYTTLTD NYTNGKLELT ALIDNNFESS IRGYQLQVQL TDDAQNSLLD EMLDVNRVSS
NESKKVTYSA QVSSPKLWSA EQPNLYNLKL TLLNSDGQAI EHIGHKLGFR STELKNGNIL
INGKPVLFKG VNRHEHDPVT AHVVSRESML KDVQLMKQFN INAVRMSHYP SDPYMYYLAD
LYGLYVMDEA NTESHGIGAA NQGAAYDPQN HLVNKPEWAA AYIDRVSNMY HATKNNPSVV
MRSLGNESGD GPNLEATFDW LKKQEPNTPV ISEQAQMRRH TDAYGQMYAP IDDIERYARR
KLDTTRPVIL IEYEHAMGNS LGNFKEYWDS FEKYPSLQGG FIWDWVDQTF AMKTLDGTPY
WGYGGDLEPA ATVTSLSFAA NGLVYADRTP YPYLWEVKNV HQNVGFSSDD IENGKLTITN
KHYFASLEGQ SLSWQLLANG EKVAQGEGIP LTAQPQQQQV VSLNYVISRE PGVEYFLDVQ
VTSDTENGLV PKGHITAWSQ LALPTIEASE EKPDEVRLSV SDKKEEYRFK GKDFSLVIDK
TTGLISSMEY FKDELLKASP RPDFWRAPID NDLPIRGYGD KFGPWQKAGK NTKLTSIKLI
KESRYLAKVE VEHYLSAVGS RYFTTYNIHG NGEVKVDVYF YAAPHKQQSE IPRLGTLFEL
DQEYENVAWY GRGPHENYSD RQTSAHVGLY QSSVDDLYVP YVRAQENGYR SDVRQVHFYN
QKGEGVTFEG EPLLGFGAQY YDTDDYHASA GQAKTKNIHP HDLPRKERIF VNIDYLQRGV
GGTNTWGAKP LSDYIIPFLD YQYSYSFKPF KK
//
