ID R5GSM1_9BACT Unreviewed; 1343 AA.
AC R5GSM1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=BN773_00081 {ECO:0000313|EMBL:CCY15551.1};
OS Prevotella sp. CAG:755.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262935 {ECO:0000313|EMBL:CCY15551.1, ECO:0000313|Proteomes:UP000018353};
RN [1] {ECO:0000313|EMBL:CCY15551.1, ECO:0000313|Proteomes:UP000018353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:755 {ECO:0000313|Proteomes:UP000018353};
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:CCY15551.1}.
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DR EMBL; CAXR010000068; CCY15551.1; -; Genomic_DNA.
DR STRING; 1262935.BN773_00081; -.
DR Proteomes; UP000018353; 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; 2.
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; IPR000421; FA58C.
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; PF00754; F5_F8_type_C; 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 SMART; SM00231; FA58C; 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; 2.
DR PROSITE; PS50022; FA58C_3; 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:UP000018353};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1343
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004380674"
FT DOMAIN 1191..1340
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1343 AA; 151399 MW; 5AAD730D0A42E24A CRC64;
MMRKLTLGLL AAALSWPAYA DVQPLAGFRY AAEEAPTGRE WQSPEDLALN KEQPRARFFS
FADTESARKV LPEHSSYWMS LDGTWKFNWA KNPDERPKTF FDPAFDTSGW DDVQVPMCWN
VVGIQKDGSL KYGVPIYSNQ RVIFQHELKV DDWRGGVMRT PPQDWVTFKD RNEVGSYRRT
FTVPAEWDGR EVYINFDGVD SFFYLWINGH YVGFSKNSRN LAAFNITDFL QKGENTVAVE
VYRSSDASFL ESQDMMRLPG IFRSVSLTSK PQVHVRDLVV IPDLDNDYVN GSLTITADVR
NLSKKKAKGY KMTYTLYANP LYSDETRLVD GVGAEVEVNE VASGHSEAAR TVLYVTNPMK
WSAEEPWRYT LIGELKDKKG RTVETVSATV GFRKVEIKDT KAEDDEFGLA GRYFYVNGRT
VKFKGVNRHE TSADRGHAIT HEQMEKEVML MKRANINHVR GSHYPDNPYW YYLCNKYGIY
LEDEANIESH EYYYGKESLS HPVEWRAAHI ARDMEMVHAN VNDPAIVIWS LGNEAGPGEN
FVHAYNAIKA FDTSRPVQYE RNNSIVDMGS NQYPSINWMW QAASGKLPIK YPFHISEYAH
SMGNAVGNLV DYWNAIESTN YICGGAIWEW IDHGLYYYDK TSGRRFIAYG GDFGDKPNDG
IFCMDGLMNA DLTPKPQYYE VKKVYQNVDV LPVDMTKGQI RVANENYFIP IDRNYEMTWT
LFKDGLPVDS GNAFRGPRME LGPRDTLSYS IPYDYASLEP QSEYFVKVQF RLRQDMPWAK
KGYVQMEEQL LVKEATGWPA IASVAKGGKL SVADEKDFIT VKGDQFTARF DKKTGTIYDL
TYGTDKVIAD GNGPKLDAYR AQVDNDNWAW NAWIQNGLHN MAHRALSSDS YTRKDGAVVV
SFNVESQAPY KSTIRGGAAA GPYKLTEHKD QPTGPDDFKF NSQVTWTVYA DGSIELSSSI
TSNNSELDLA RIGYSFQVDP KYSRYTYYGR GPLNNYNDRK TSQFVERYES TVKDQFVNHG
KPQDMANREE VRWAALTDAS GHGIQFVSTG KLSTSVLPWS ALELMLAPHP YQLPESHTTH
VNLDAAVTGL GGNSCGQGSP LPKDHVKAVP HIVGFLLRPT NGADLTTNAA VTSSGDQTPI
ISRDRKGNMT VSGTREGATI MYAVGKEKAK AYEGTRNLRT GGTVTAWYED MPQVKMTMTF
PRIENIPMVV VETTSQESGE GNASHLVDGN PNTYWHTMYS VTVAQYPHSV TFDASEEKNI
KGFTYLPRQD SRNGNVKGYK VQVSKDGKTW GDPVAQGEFA NDQKLKRIML AKPVKARFVR
FTATSSQDGQ DFASGAEFGV LEE
//
