ID A0A399T2M3_9BACT Unreviewed; 1255 AA.
AC A0A399T2M3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=D1614_06440 {ECO:0000313|EMBL:RIJ49194.1};
OS Maribellus luteus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Maribellus.
OX NCBI_TaxID=2305463 {ECO:0000313|EMBL:RIJ49194.1, ECO:0000313|Proteomes:UP000265926};
RN [1] {ECO:0000313|EMBL:RIJ49194.1, ECO:0000313|Proteomes:UP000265926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XSD2 {ECO:0000313|EMBL:RIJ49194.1,
RC ECO:0000313|Proteomes:UP000265926};
RA Zhou L.Y.;
RT "Pallidiluteibacterium maritimus gen. nov., sp. nov., isolated from coastal
RT sediment.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:RIJ49194.1}.
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DR EMBL; QWGR01000003; RIJ49194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A399T2M3; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000265926; 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 CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
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; IPR013320; ConA-like_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 InterPro; IPR006558; LamG-like.
DR InterPro; IPR001791; Laminin_G.
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 Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
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 Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000265926};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1255
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017451300"
FT DOMAIN 639..773
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 955..1253
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1255 AA; 143135 MW; 0D7BBB1E3F30876F CRC64;
MNRIALLLLV LLPAGLLAQQ VEFLPDDWQN PAVFEKGQNL PHAFHIPYSS RERAIQDLPR
KCENYQLLNG TWKFLWVETP DQVPADFWNP DFELNGWNEI TVPSNWQMEG YGHPKFRNVA
LSFESDPPKI PEYYNPGGCY KRKFELPENW GEKEVMLRFE GVKSASYVWV NGEKVGYNQG
GFEPAEYNIS RFLKKGENDL SVEVLRFSDG SYLENQDMWR LSGIFRDVKL YAQPQTYIHD
HYVTTDLDEE YKDATLKVEV DLTNTLPEKR EVSIEMDVLD DEGRSILAEG IQKETAAVDS
ASIKKVTLST VVVDPTKWSA EFPHLFQLLI ILKDKDGNTL EALSQKIGFR EVKYKDHILT
VNGAPVKLNG VNSHMHDPKH GQAVPQETLR TDLILMKQHN INCVRTSHYP PTPEYIALAD
ELGMYIFDEV GDEAHNNIHL SENRAWTEMY RDRSRKLVYR DRNRPSVIVW SAGNESGSGE
NIHEVIKTGK AIDPSRPVWM YGGNTFYIPF EDIVGPRYWS PIDYKNLAEG KVLPENDQRA
SFMDEYLAAT GNGLGGMDEY WEYIWKYPRL TGGAIWDWIS PGIETPRRIL SDLSEAKNDG
QIMGRPVFAE GKNGWGLEFS GHDDWVEFYR DPSLDITGNQ LSISFWVKPF EIPQPNTFIA
KGGHGYGIGM EDPRTLEFYL QSGKRVSAKA KVNSDFYGNW HHIAGIYDGR SLQLYIDKKQ
VATSSFSGNI SSTPFPLCIG REAETQDQGE YSGRLSKMVI DDVKIFPEAV RVGNIEHQTD
GAVLHLDFEK DTTAGSFYAV GLGGRTYGIV WPDRTPQPEI NQIKKSGQPV KIEVIDMAAG
RIQVINRHQF KNLKELDGRW ELRVDGKPSQ RGIFECEAAP GDTVEVTIDY RRPRIDSREE
CLMLVSFVLK EDQSWAPKGH EIAWEQFKVS TDLYFVEEKP NDRKVSFSES KDKVVITGDD
FSYVIDKSTA KLSSLQFKGT EYLEGGPVFN VWRAPTANDL DPWGSYMFSS DNRTPGYGRS
IDNQLRTLGM RDLLTQVDEV DVIQLNEKEV KVRMKVFSNS SLPANRRLNR GGLFSAFERN
ETWTFSASGK IDLEQEIIPH GPMPDMLPKI GLQFELPKAF SAVEYYGRGP FENYPDRKTG
AKVNWYHSTA DSMYVPYIIP QEYGNRSDVR WLKVENADGK GLLIKGDDWL NFSLHKYSTD
NLSRAMYTYQ LKEAPNTILN VDFEVSGVGG TAIRQLQKYR VRPGVRNYKL SITPF
//
