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
//