ID A0A249T115_9BACT Unreviewed; 1067 AA.
AC A0A249T115;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CK934_22815 {ECO:0000313|EMBL:ASZ13578.1};
OS Chitinophaga sp. MD30.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ13578.1, ECO:0000313|Proteomes:UP000217148};
RN [1] {ECO:0000313|EMBL:ASZ13578.1, ECO:0000313|Proteomes:UP000217148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD30 {ECO:0000313|EMBL:ASZ13578.1,
RC ECO:0000313|Proteomes:UP000217148};
RA Wan X., Darris M., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT biofilm in an air conditioner condensate pipe.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP023254; ASZ13578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249T115; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000217148; Chromosome.
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; 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.
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:UP000217148};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..1067
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012715921"
FT DOMAIN 776..1050
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1067 AA; 121287 MW; E55284790AF92EA4 CRC64;
MISLIHLPLA AVLKTAANAF AAKKYLQLMI CIACYCWPMT ALAQQPDWEN PRHTSQGTLP
PRAHFIPFAS RETALRQTLP SPWVQSLDGK WKFNIVSNPS LRPTGFQLPS FNDAAWKEIN
VPANWQTAGF DSYIFTDVEY PFPPNPPKVP AAFNPVGSYR RSFQVPAHWK NKQVWIQLGA
VNSFFYIWIN GQYLGFSKDS KTPATFNITP FLRKGNNVLA LQVFRFNDGS YLEGQDMWKL
SGIERSVYLL ARPPACVYDF FAQPSLVNNY RDGRLQLQLT LNQQPGSTAA GQQLEVQLLD
KNKVLLSRQW LPAKDTVWNM DAVIPNISAW SAEHPNLYTL LITHKDKQGK VLETIAHQLG
FRNVEIKNGL FLVNGAPIKL KGVNRHEHDM YNARVITKEE MIRDIRTMKE YNINAVRNSH
YPCNEEWYEL CDRYGIYVLD EANIECDGMS LHPMKTLSDN PDWEAAYLHR TRRMVQRDKN
YTCIVTWSLG NESAFGNNFK TTYNYIKSVD PTRPVQYEGG GDNAWTDIYC PMYKPVNVLK
RYVQQQQQKP LILCEYAHMM GNSGGNLLDD WELIYQHPQL QGGFIWDFAD QTFKRKDEQG
RDIWAYGGDM GTVGATSDTS FCADGLLAAD RSPHPQAFEV RKVYQYIRIT PVDSSMQQWR
IQNHYDFTNL SAYTLRWSLR ADGRHITAAN MPPIQLRPGT DTVVTIPLPP IHPQPGVEYF
LHWQASTNAA APLLPKGWVA ATEQYRLPAY QPIRLQRLNT AMLSTLRVQD TADELRIGND
HFTAAFSKTR GWLHQLVANG TALMASPLMP HFWRAATDND IGNSMQIRAA VWQHAADSAV
LQAITASIQD SFRITISTRH FLPTVKVQYN TSYRILANGD INVSVDFLPA DTTMPELPRI
GMRMSVLPAY DNVSWLGRGP FDNYADRHFA AEVAVYSAKA DALFHPYPRA QESGYRTGIR
WVALQAANKS GWIMTSDSLM NTGILHFNQQ RLDFDRSRNK HGGSMTNEPL ITWNIDYRQS
GVGGDNSWGA KAHPQYRIPC RNYHYSFLLR PLPAGANAGT LAKERCE
//
