ID R5V8M9_9BACT Unreviewed; 1017 AA.
AC R5V8M9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=BN754_00273 {ECO:0000313|EMBL:CCZ77007.1};
OS Alistipes finegoldii CAG:68.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1263035 {ECO:0000313|EMBL:CCZ77007.1, ECO:0000313|Proteomes:UP000018154};
RN [1] {ECO:0000313|EMBL:CCZ77007.1, ECO:0000313|Proteomes:UP000018154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:68 {ECO:0000313|Proteomes:UP000018154};
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 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}.
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:CCZ77007.1}.
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DR EMBL; CBAO010000240; CCZ77007.1; -; Genomic_DNA.
DR AlphaFoldDB; R5V8M9; -.
DR Proteomes; UP000018154; 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; IPR023232; Glyco_hydro_2_AS.
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.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1017
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004406845"
FT DOMAIN 738..1013
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1017 AA; 114944 MW; FFB3948BFA6D02D8 CRC64;
MKKTLLILAA ALSGALAASA QTGREWQDLA VNEINRLPMH STFAAGESMP LDGVWKFHWV
RNASERPSGI WQEDYDDASW GAMPVPGMWE LNGYGDPLYV NVGYAWRGNF ENDPPHVPDA
ENHVGSYRHT FEVPASWSGK DIFLSIGSAT SNVYVWINGR FVGYSEDSKL AAEFDVTKFV
KPGENLIALQ MFRWSDGTYL EDQDFWRFSG IARGVTLTVR DKAHLKDVRI TPTLDADYRD
AQLHVEVETT PRVKSVGLTL LDAAGEAVTE QQIRPAGGKA GCLFRVADPA KWSAEAPNLY
TLRIDVSDGR NVTETVTQPV GFRSVEIRNA QLLVNGQPVL IKGADRHEMD PIGGYVVSRE
RMIEDIRIMK EMNINAVRTS HYPNDPQWYE LCDEYGIYVV DEANVESHGM GYGEETLAKV
PAFAQAHMER NQRMVLRDKN HPSVIVWSMG NEAGMGPNFE ACYRWIKDYD ASRPVHYERA
VYDRDGAFTD IICPMYWDYA QCEKYLKNNP SKPLIQCEYA HAMGNSMGGL DHYWKLVRQY
PSYQGGFIWD FVDQGLARYE KNGRVSFLYG GDFNNYDATD NSFNCNGIIA PDRTWHPHAY
EVKRQYQNIW TELLDPAQGR VEVYNENFFV GLDDYELTWE LVVDGRVVKA GRIGELDVAP
RQRRTYALGF TSADFCPQAK ELLVNVAYKL KNKRPLLDIG HTAAQQQFVV REYDCKAGFG
LAASERPVEV TVWERGTRVA GQTWEMFFSR DGFLSAYDVD GRALMAEGAE LRPQFWRAPT
ENDLGAKLDR KLAVWKNPEL KLTKFDAGVK DGVAVVEALY ELPAVKATLA LTYRINGAGE
MEVTERMTAD KSAEVPNLLR YGMTLTMPAR YDRVIYYGRG EHENYADRLS SADLGLYEQR
VADQYHDEYV RPQESGTKSD VRWWTVADSS GTGLTILSDA PFSASALPYA TADLDVSNFP
PQQHSGTLTA RDATFVNFDL RQSGLGCIDS WGQLPEERFR VPYGDYTFRF LLRPTIK
//
