ID R6WNP6_9BACT Unreviewed; 938 AA.
AC R6WNP6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BN725_02086 {ECO:0000313|EMBL:CDD05681.1};
OS Prevotella sp. CAG:592.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262931 {ECO:0000313|EMBL:CDD05681.1, ECO:0000313|Proteomes:UP000018343};
RN [1] {ECO:0000313|EMBL:CDD05681.1, ECO:0000313|Proteomes:UP000018343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:592 {ECO:0000313|Proteomes:UP000018343};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDD05681.1}.
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DR EMBL; CBGI010000185; CDD05681.1; -; Genomic_DNA.
DR AlphaFoldDB; R6WNP6; -.
DR Proteomes; UP000018343; 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; 1.
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 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 PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018343};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..938
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004435539"
FT DOMAIN 56..195
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 208..297
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 305..529
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 670..863
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|Pfam:PF02929"
SQ SEQUENCE 938 AA; 105789 MW; 13EB98CF7AF8B11D CRC64;
MKQTIISALA LLSASIGATA QNDVMTHRQY LSGHGCDDMV QWDFFCTGGN NSGKWTKIGV
PSCWELQGFG NFQYGMKFYG KAFPDGIADE KGMYKYEFKL PKEWANHHIE LVFEASMTDT
QVMINKRKAG SKHMGAFYRI TYDVTDRVFF GDKKNLLEVT VSKESENAGV NLSERRADYW
NFGGIFRPVF IVCKPALNIE RTAINATADG EFNAYVLLNH TIEGAKVKTT ISDMNGKKVA
ENTTDVRHGS DYADVAFKVS NPKLWTAETP NRYQVAFSLI DAYGKTLHVE KDKFGFRTIE
TRESDGLYIN GKKVNIRGVN RHSFRPETGR TLSYQKNLED VELIKSMNMN AVRLSHYPAD
PEFYDICDSL GLYVMDELSG WHGHHETING QKLIREMVTR DVNHPSIIWW SNGNEKGWNT
ELDGDFHKWD IQKRPVLHPQ GNFSGYETMH YRSYGESNEY MRKPEIWMPT EFLHALYDGG
AGAGLYDYWE VMRQWPRCAG GFIWALVDEG VKRVDMGGMI DNVGNYGADG IVGPHHEKEG
SYYTVKQIWC PVQVSMPEHF DGRLNVENRY NFLSLKGVKF DYSYLKYNGS KASSLKQGVV
NGADIPADSK GTISVPAVPN GAEALSVKAT DQYGKDLFTW VFKLKDSDKP FAKTATTGNR
PQMNGGVVKA GNVTFTFNEK DGSLASVTTK KGDYKFGNGP KFFAYRRADR SMDQFYNHDD
PQAEKKKTTY EEYAEQGKFD NLTATEGAND TLIVTATYKL GSLQKAEWHI APDGGARLVY
SYIFNGVVDL MGVKFDLPET EVKHKEWLGC GPYRVWKNRI HGPQLGVWAN DYNDPVPGES
FDYPEFKGYF AGVQWMKLQT KTGMITICPG TDKDYVGVYQ PRDGRDQLLY TLPETGISMM
QVIPAVRNKV NTTDLNGPSA QPVWANGSYT GEVTLHFD
//
