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Database: UniProt
Entry: U2MJ99_SERFO
LinkDB: U2MJ99_SERFO
Original site: U2MJ99_SERFO 
ID   U2MJ99_SERFO            Unreviewed;      1023 AA.
AC   U2MJ99;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=L580_0442 {ECO:0000313|EMBL:ERK16863.1};
OS   Serratia fonticola AU-P3(3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1332070 {ECO:0000313|EMBL:ERK16863.1, ECO:0000313|Proteomes:UP000016623};
RN   [1] {ECO:0000313|EMBL:ERK16863.1, ECO:0000313|Proteomes:UP000016623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU-P3(3) {ECO:0000313|Proteomes:UP000016623};
RX   PubMed=24233592;
RA   Devi U., Khatri I., Kumar N., Kumar L., Sharma D., Subramanian S.,
RA   Saini A.K.;
RT   "Draft Genome Sequence of a Plant Growth-Promoting Rhizobacterium, Serratia
RT   fonticola Strain AU-P3(3).";
RL   Genome Announc. 1:e00946-e00913(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         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:ERK16863.1}.
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DR   EMBL; ASZB01000001; ERK16863.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2MJ99; -.
DR   PATRIC; fig|1332070.3.peg.445; -.
DR   Proteomes; UP000016623; 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; LACTASE; 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}.
FT   DOMAIN          723..994
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1023 AA;  117087 MW;  59CFE34F0041B3C6 CRC64;
     MNNWENFQHL HENRMAPRAY FFSYDSLKRA QTFQRALSSH FMALSGQWSF NYFTNPLRVP
     EDFYSQRMTD WGQITVPNMW QMEGHGVLQY TDEGFPFPID VPFVPTDNPT GAYQRSFTMS
     EQWNGKQTII KFDGVETYFE VYVNGQYVGF SKGSRLTAEF DISGYVRSGE NLLAVRVMQW
     ADSTYIEDQD MWWTAGIFRD VYLVGKEPVH VQDLTVRTDF AADYQSAILS CVLEIENLSG
     TPLADYVIEY ALFDNDNLLV QQSLGAQTQT HFAINLENPI QWSAENPYLY QLYITLKDQN
     GTVLEVIPQR VGFRDIKVRD GLFYINNQYV MLHGVNRHDN DHLKGRAVGM DRVEKDLILM
     KQHNINSVRT AHYPNDPRFY ELCDIYGLFV MAETDVETHG FANVGDLSRL TNDPAWETVF
     VDRIVRHVHA QKNHPSIVMW SLGNESGYGC NIHAMYHATK AIDNTRLVHY EEDRDAEVVD
     IISTMYTRAP LMNEFGEHPH AKPRIICEYA HAMGNGPGGL TEYQNVFYQH DHIQGHYVWE
     WCDHGILALD EQGQAFYKYG GDFGDYPNNY NFCMDGLIFP DQTPGPGLKE YKQVIAPVKI
     RALEARLGTF LVENKLWFTN LDDYTLTAEI RAEGETLATR SLRLKDLAAN SSREIRLELP
     ELDEREAFVN FTVRKNSSTL YSPANHDIAV YQFQLKENTA QAEAYTNLNA LPLRVAESRL
     AYSISGQDFT LTFSKVNGKL TSWISNGAEI IASAPTLSFF KPMIDNHKQE YQGLWEPAHL
     QIMQEHFRTL DVVQADGRVE ITVTSIIAPP VFDFGMRCCY RYQINAEGQL NVELSGERYG
     DYPYVIPAIG LDVGINGGFD RVNYYGRGPE ENYQDSQQAN LIDIYQTTVA EMFEHYPFPQ
     NNGNRQHVRW AALTNRHGTG LLVKPQQPIN FSAWQYTSQN LHQAQHTNEL QPSGYITLNL
     DHQVMGLGSN SWGSEVLDSY RVYMAPFRYG LTLMPLQAGD VSAQALANHD FANDFFTPTT
     NEA
//
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