ID A0A1K1PG05_9BACT Unreviewed; 1496 AA.
AC A0A1K1PG05;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN02910409_0075 {ECO:0000313|EMBL:SFW46371.1};
OS Prevotellaceae bacterium HUN156.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae.
OX NCBI_TaxID=1520830 {ECO:0000313|EMBL:SFW46371.1, ECO:0000313|Proteomes:UP000182805};
RN [1] {ECO:0000313|EMBL:SFW46371.1, ECO:0000313|Proteomes:UP000182805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HUN156 {ECO:0000313|EMBL:SFW46371.1,
RC ECO:0000313|Proteomes:UP000182805};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FPIT01000012; SFW46371.1; -; Genomic_DNA.
DR STRING; 1520830.SAMN02910409_0075; -.
DR Proteomes; UP000182805; 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; 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:UP000182805}.
FT DOMAIN 784..1052
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1496 AA; 168424 MW; 55ACA5751BD76370 CRC64;
MAQSDETEQT DQSTPHWEDP EFFEENKLDG HATFMPYTST EDMKGDSRYE KPWVTPEKAS
FLSLNGVWKF CFVSDAKERP GSSFYADEAS VRRWDDIEVP SCWEMKGYDK PVYANVNYPF
EDNAPYIKLR QEFKGKLGEN PTGSYRRTFV LPEEWMDKRT VLHFDGVYGA CYVWVNGQYV
GYSQGSNNDA EFDLTDVVRT GENNISVQVI RYHDGAYLEG QDAWHMSGIH RDVYLYATPK
TYVADHVLTA ELNAANNYQS GTLNVKVAMK TIEYEASDKS IEVELRDDDD VLIKSTSASV
SPSSVVDLQL SGLTDLHLWS AETPYLYHVV VRQKDNDGQE EMVFSTRYGF RQIEQRGQLV
YINGQRIYFK GVNTQDTHPV TGRTMTVEAL LEDVTMMKQA NVNTVRTSHY PRQPKMMAMF
DYYGLYVMNE ADIESHKDWS DHAPDGTLAS RKDYQGQYID RTTRMVLRDR NCPSVVFWSL
GNEGGLGPNF VVAYDAVRQL DNRLIHYEGH SKNQKFNDIS DINSSMYPTL SFVTQNVNGD
KPFFICEYSH SKGAGLPNMQ EYWDLIEGSS AGIGACIWDW VDQAIFNPAD LAGVDPNDKS
TWPKLNGFYK LMVGYDFPSP DPNDVTVSLN DGVITADRSW SAELNVAKHV HQYIRFKDYD
EDAKQLTITN HYNFLKLSQF KLHYEVLQNG KVVEDGDLDM PSLEPGQTTT ITLPIGIEHY
LSDEEILLNV EARLKDATAW ADAGYTMAWE QFMLKERPAT LPSVPAVADD AALLQLTESD
DVYTISGKYI SMIVSKSGEV ESLELLGHSI ITPDGAPVYS NFRYLSHDPN GERGSFLERT
NVECQLSADQ QTATVTLTSP GTRCATKFVY TLYAAGVADL QATFIPQENS SVLQNGKSNL
RRIGLKMKMP AGREKVEYYA QGPWESFVDR QSGNVLGRYT TTVSELFESY THPQSCGNRM
SLRQLRMWND EMITDGTLVI TTLGQVDFSL MHYNEENFTA KKLHPWNLSA DATIYARFDA
YQRGIGEATM NVGVLDKYRC PTTPQTFTLR FELEGAIINS AERKALKQLI DEAEAVNVPT
GNIGTGAFQF PVAPINTFKK AITDALSVYN DVTKGSEDFK GACTPLRRAL IAYAAVKDEL
NEPVAERYNI FFHYDNVSYD GYVVTMSKGT NPTQGNYGAK YLTPTVNPNY SQAFRMKKTT
GQNRYILSFI TDEGVTRWLC DGSVWDMNIA TKSAQRRIRT TIDESKALPF EIRYSEMQGH
TPRFMLVNTV VDEGIGHNNN DDMYTLQAAT FSFVEAEKAS VPVTIDAKMP LITRIFPFLP
VLPPGVKAYS CSGIVTKRGY DYMVLTEQNA PEANTPYILY APYGCDSEPL VGWGTASNPT
YTNGYLTGVY EETAVPIGSY VFNHQPDDSW GFSKVNSGFS FIDCYQVYLT APTSMGMVYF
DMQEMGINGI SDATNSSITV YDMLGRRVEP ANGNAMKKGI YVIRKGNGEI EKVSMK
//
