ID A0A0F5JNL3_9BACT Unreviewed; 1043 AA.
AC A0A0F5JNL3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=HMPREF1536_00916 {ECO:0000313|EMBL:KKB59368.1};
OS Parabacteroides gordonii MS-1 = DSM 23371.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB59368.1, ECO:0000313|Proteomes:UP000033035};
RN [1] {ECO:0000313|EMBL:KKB59368.1, ECO:0000313|Proteomes:UP000033035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-1 {ECO:0000313|EMBL:KKB59368.1,
RC ECO:0000313|Proteomes:UP000033035};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL Submitted (APR-2013) 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:KKB59368.1}.
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DR EMBL; AQHW01000005; KKB59368.1; -; Genomic_DNA.
DR RefSeq; WP_028726908.1; NZ_KQ033919.1.
DR AlphaFoldDB; A0A0F5JNL3; -.
DR STRING; 1203610.HMPREF1536_00916; -.
DR PATRIC; fig|1203610.3.peg.939; -.
DR HOGENOM; CLU_002346_0_2_10; -.
DR Proteomes; UP000033035; 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:UP000033035};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1043
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002490313"
FT DOMAIN 749..1027
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1043 AA; 118802 MW; A7786C78279B3E34 CRC64;
MKHLFYTASA LLVSLALQAQ PKEWENQRVN QINREPIHAH FVPYSSEKGA LHKDISKEQR
YSLNGTWKFH YAKNPASRPV TFYEEGYDVT DWKDIEVPGS WELQGFDAPI YTDTRYPFPA
EPPHVPTDYN PVGSYVTTFT VPADFKGKDI LLNFGGVESA YYCWINGHFV GYAEDSRLPS
EFLINKYLKS GENTLAVEVY RYSDGSYLEG QDYWKYSGIE RDVRLIARPQ ERIKDFELSA
DLVNDYQDGL LNVKVTLDNR KINKGTAVQL KVLDGMKEIA SERFTVKAKT DSLFVFTEQF
PGIKHWTAET PNLYSLVVNT LDKQGKVTES FVQRFGFRKV EMKNGMLQVN GTPILIKGVN
RHEHDMHKGR SISVESMIED IRLMKQFNIN AVRTCHYPNH EEWYDLCNEY GLYLVDEANI
ESHGMEAHPD GTLANMEGWD IPFMERMERM VERDKNFTAI ITWSLGNESG YGKHFETLYH
WTKERDASRP VQYEGGGVKG LSDIYCPMYG RIWLLRQWVN QRQPRPLILC EYAHAMGNSV
GNLNDYWDLI YKYDNLQGGF IWDWVDQTFA IKDKKGNDIQ AYGGDMGFVG IVNDSNFCAN
GLVAADRSLH PHIWEVKKVY QYMHFEGVPF SAGLIKVTNR HDFVSSDVYD YVWTVKADGK
IISQGKLDVP VIAPHQSVEV PVQIPAIKGE PGTEYFLHIS ALTKEETPLV LKGHLAASEQ
WKLPVVSSSV SVPVSSETLS TMDEAENMTI KGKALSVVFS KKNGEITSYA VDGNDYLLEG
LRPNFWRPLT DNDVANKLGS RSETWKNAGN ELVVKEFSAD VSTDKKSVIV KVSYDMPLQE
SSCSVIYTVY ADGIIKTAYS FVPGEKQLPE IPRVGMRMIL KGEYDQMTWF GRGPQENYWD
RKSGADIDLY KASVWDQYHP YVRAQETANK SDVRWVALQN QAGNGILVKS ACLPLGISAW
NFPMKDIEYI PSSIQHIHGG SIEKKDMVWL NIDKQQMGVG GDNTWGAQTH PEYTITPVSQ
EYSFFIIPVD KQTNLVEISK LNR
//
