ID R9PKS9_AGAAL Unreviewed; 1040 AA.
AC R9PKS9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=AALB_2064 {ECO:0000313|EMBL:GAD01984.1};
OS Agarivorans albus MKT 106.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD01984.1, ECO:0000313|Proteomes:UP000014461};
RN [1] {ECO:0000313|EMBL:GAD01984.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT Marine Bacterium.";
RL Genome Announc. 1:e00367-13(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 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:GAD01984.1}.
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DR EMBL; BARX01000012; GAD01984.1; -; Genomic_DNA.
DR RefSeq; WP_016401752.1; NZ_BARX01000012.1.
DR AlphaFoldDB; R9PKS9; -.
DR STRING; 1331007.AALB_2064; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000014461; 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 Reference proteome {ECO:0000313|Proteomes:UP000014461}.
FT DOMAIN 757..1037
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1040 AA; 117416 MW; 58910EC075806211 CRC64;
MTRVSATLLA QKDWENPSVT ERNRLPSHVP LASYSGLDAA LNLQQAEHQL SLNGQWNFCL
LKQPEQLSDA LIAGSKGSWK SIAVPGNWQL QGFDKAIYTN VIYPFEVNPP YVPSDNPTGV
YRTEFNYQAA WANKQVRLRF EGVNSAFHVV INGQQVGYGQ DSRLASEFDI GPFLQEGTNQ
LCVIVYRWSD GSYLEDQDMW WLSGIFRDVS IYAKPQVHIA DFSIHTQLDA CYRDAQLQVE
VQLAGASLAQ LDGYQIELQL YDGDGAVFAN PVRESTNNLS VDEKGGFADR IFLSSTVVEP
KLWSDEQPNL YRAVLSLLDA KGNVLEVEQS SVGFRCVEIS DGLLKLNGKP VLIRGVNRHE
HDPELGHVMT EATMLQDIKL LKQNNFNAVR TAHYPNHPRW YELCDEYGLL LVDETNLETH
GMFPMKRLSD DPQWMHAYMQ RVTRMVARDK NHPSIIIWSL GNESGYGSNH DAMYGWLKQA
DQSRPIQYEG GGADTPATDI LCPMYARVDW DTAGEGIPKR AITAHIADPN EQRPLILCEY
AHAMGNSLGS IEEYWRAFRL HPRLQGGFIW DWVDQGITKQ SDSGETYWAY GGDFGDQPND
RQFCINGLIF PDRSPHPSLH EIKYLQQYWQ ISAENLAKGE VLISNEHLVN DSSNTAGEWR
IERNGELFSQ GEFSLSLQAG EQQIMCLPKA AMQDLATQTS GEFWLTINIK LKQATAWALA
GHSLAKQQFK LAFGGLNSPK PLNKAEVKCT QQDRRIRFES SKQLLEFDCV SAQWLAWTVN
EKQLFTAAPV DNFYRAPLDN DIGVSEASQM DPNSWIARWQ SAGLHQLKRE ALDFNFSQLS
NGCWLVECSS EYRHQQKTAF KVLHRYVISA DKVAFDCEVN AAAYLPPLPR VGLSLSLDKQ
FSELSWFGLG PHENYRDRLA AATVSRYSET VDNLHTPYIF PSENGGRGEV RQLSLKHEQQ
LNVELHCQPS LQMTASRFSQ QDLSDATHNY QLKDSGSVFV HLDVAHQGVG GDDSWSPSVH
PKHQVLENYF SYHIDFTAQG
//