ID A0A0Q4GLE4_9SPHI Unreviewed; 1054 AA.
AC A0A0Q4GLE4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=ASE74_13760 {ECO:0000313|EMBL:KQM78563.1};
OS Pedobacter sp. Leaf216.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM78563.1, ECO:0000313|Proteomes:UP000051744};
RN [1] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Garrido-Oter R., Mueller D.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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}.
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:KQM78563.1}.
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DR EMBL; LMKM01000003; KQM78563.1; -; Genomic_DNA.
DR RefSeq; WP_055903632.1; NZ_LMKM01000003.1.
DR AlphaFoldDB; A0A0Q4GLE4; -.
DR STRING; 1735684.ASE74_13760; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000051744; 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; IPR006103; Glyco_hydro_2_cat.
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.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KQM78563.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1054
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006219059"
FT DOMAIN 774..1051
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1054 AA; 120558 MW; A27808C585772ECA CRC64;
MNRKLVVLFT FLGFAGQISA QDLPSETQTP EVVSLNRLPM RASAFAFENQ ELAAKKAKEK
STYFLSLNGT WKFNWVKDSR KRPTDFYKVD FDDKSWDNFK VPANWELNGY GTPIYVNQPY
EFAGRQLTGA KMNPPFDIPV DNNPVGSYRK KINIPANWDG KQVFISLGAV KSAFYIWVNG
KKVGYSEDSK LAAEFDITKY VKPGENTIAL QVYRWSDGSY LECQDMWRIS GIEREVYLYA
TPKLDIRDFK VVGGLDASYT NGLLNVDLSV ENYKIDQRTN HSRPDSFYVA LDLIDAKGNN
IWKDATTIQK VLGNYKTDLS FKTQINNVKN WSAEIPYLYT LYITLKDKNN KIIEVIPQRV
GFRSVEIKGS DLLVNGKRVF LKGVNRHEHN ATQGHTLTHA DMEKDMEMMK RLNVNAVRHS
HYPPDPYWME LCDEYGLYVI DEANIESHGR YYSLETSFAN DKQWRIPHLE RITRMYERDK
NHASVITWSL GNEAGNGVNF YEAYQWLKGK DFRPVQYERA ESDFNTDMIV PQYPSPNYLP
RYSKQDKETR PFIMSEYAHI MGNSLGNFKE YWDAIENNPK LQGGFVWEWI DQSIDTVKNG
KRIMAYGGDF PLSGPVDENF SDNDFCVKGV VTAYRGMTPM AVELKKVHQY IKTTFNGTNQ
INVNNSYFFK DISNVQLNWE LVEDGKVIQT GVVSNLNIGP RQTQMIQIPF KTNYAIGKEY
FLNVHYRLKT AEPFLEKGYE VAYDQIALAG APKANVYSSN KKALKVDQTA EKAVVKGSDF
TITFDLIKGT LLSYISKGQE LLASGPQPGF YRAPTDNDIG AGLNTKLRMW SNVYQDNDAG
HIKATVNSTA DGFTLTITSS LLKGDAETTQ KFEVFGDGTI KVDNQFKAIT GNYKSLMRIG
NDLQLKNDYS NIQWYGRGPG ENYIDRKTAS LIGNYKSTVA DQYFAYARPQ ESGNKTDVRW
VAFTNKAGKG LRFEFADQLL SFNALPYSVE DLDPEAEKKQ YHSGELVKRN QIYVHMDMQQ
LGVQGIDSWG SMPLIQYQIP FKDYHYSYYI KPIK
//
