ID J3AVK9_9CAUL Unreviewed; 1074 AA.
AC J3AVK9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=PMI01_00194 {ECO:0000313|EMBL:EJL38269.1};
OS Caulobacter sp. AP07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL38269.1, ECO:0000313|Proteomes:UP000007300};
RN [1] {ECO:0000313|EMBL:EJL38269.1, ECO:0000313|Proteomes:UP000007300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP07 {ECO:0000313|EMBL:EJL38269.1,
RC ECO:0000313|Proteomes:UP000007300};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL38269.1}.
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; AKKF01000008; EJL38269.1; -; Genomic_DNA.
DR RefSeq; WP_007661791.1; NZ_AKKF01000008.1.
DR AlphaFoldDB; J3AVK9; -.
DR PATRIC; fig|1144304.3.peg.175; -.
DR Proteomes; UP000007300; 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; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1074
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003762825"
FT DOMAIN 783..1058
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 24..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 118435 MW; 298876DED7E96E02 CRC64;
MTGLSTRLML SSALILALGA VGAQAQTPSP PPKPIQPQIS ADRPDWENPA VFARNKQPAR
STGFPFESRD LALAGDMSAS KRFSSLNGDW KFAFSPGVDQ RPKDFWRDDF DVSGWKSIKV
PADWQAEGYD QPRYNNIVYP FAANRPLIPH ATNPVGSYRR DFTVPADWNG KDVILHIGAA
NSAFYVWVNG KSVGYSEDSK LPSEFDVTPY LRAGANNVSI EVYRWSDGSY IEDQDFWRVS
GIERDVWLMA APATRARDVF AKASLDKTYR NGQLSVDVDI ARPKPGTKVR ATLLDGDRVV
LTRDAKPATD GKASITATVP DVRTWSAETP NLYTLLIETV GADGAVLPAT SNKVGFRTVE
IKDGQVMVNG HPIIIRGVNR HEHDPDTFHV ISEASMRKDM ELMKRNNINA VRTSHYPNDE
RWYALADEYG LYVMDEANIE SHEYLSMGED KPAEREIYEL GFDPAWEAAH VSRVANMVER
DKNHPSIIFW SLGNEAGTGP TFEKAAAWIR KRDPSRLISF LGWSVLDDTH SPNAYADIYA
PMYDQFDKLI DYANDPRFTQ PLIQCEYAHM QGNSGGVLKD YWDVIYAHPK KLQGGFVWDW
VDQGMNGKDA EGRPFWKTGG DYGPNPGGDI EFGDGLNQPD RTPNPQLHEL KKVYAPVAFE
AVDAAAGRFK LTNRHDFRDL SGFDLQWELL EDGKPVAHGQ LPPLKTAARA TEDLTITLPA
PSAPGVERIV TLRARAKADS IPLVPADEVV AWDQFVLPTT TSRPTPLAPK GQVVATQDAQ
GVRLATKDAE LVIDPKTGLV TRYVLAGKTV LTGGAPNFYR ALTDNDLGAG VDKTHAAWRR
YSEERDVRSV TVQPLPGGGQ AVAIEYVLGA GAVRFLSTYA MANDGAVTVT GRFTPAKEDL
PDPLRVGLAF SMPTTMTDVA WYGRGPHETY SDRKWSGAFG LWHGKIANQN HDYMRPQETG
NKVDVRWMDI GNGQAPGVRI TGAAPLSMNV LAFPYEDLQR HPPGTWRSSD IRPHDHVSLL
VDAAQVGIGG DDTWSLKARA HMKYRIPLAP QTFSFTLSAS TIDRTATGQG GGAD
//
