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Database: UniProt
Entry: L1MMY5_9BACT
LinkDB: L1MMY5_9BACT
Original site: L1MMY5_9BACT 
ID   L1MMY5_9BACT            Unreviewed;      1308 AA.
AC   L1MMY5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=HMPREF9999_00682 {ECO:0000313|EMBL:EKX92623.1};
OS   Alloprevotella sp. oral taxon 473 str. F0040.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Alloprevotella.
OX   NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX92623.1, ECO:0000313|Proteomes:UP000010460};
RN   [1] {ECO:0000313|EMBL:EKX92623.1, ECO:0000313|Proteomes:UP000010460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0040 {ECO:0000313|EMBL:EKX92623.1,
RC   ECO:0000313|Proteomes:UP000010460};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-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:EKX92623.1}.
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DR   EMBL; AMEK01000042; EKX92623.1; -; Genomic_DNA.
DR   RefSeq; WP_009436639.1; NZ_KB290710.1.
DR   STRING; 1035197.HMPREF9999_00682; -.
DR   PATRIC; fig|1035197.3.peg.560; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_0_2_10; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000010460; 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; 2.80.10.50; -; 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   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
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   Pfam; PF14200; RicinB_lectin_2; 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   SUPFAM; SSF50370; Ricin B-like lectins; 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   Reference proteome {ECO:0000313|Proteomes:UP000010460};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..1308
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003954304"
FT   DOMAIN          943..1214
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1308 AA;  147337 MW;  0B87BB86AC965606 CRC64;
     MKTKTFSSLL TLVAIGVLWC CGALSASAKL EAERYYTLTN VHHGMTLSTG GVGAKDSPLV
     GEAYKKGSPD QLWQLKASGS DAFALYNPES NLAVDLAIQA KKNPLLWSLD VNNPNQQLIL
     EEEGTNFRLR AASFQFEARY LSITRDGKVL LDSNKNNNSL FKFTEVNLKD IQYPDRAEWE
     NEMIFGINKE RGRATFIPYA TTAQLQADAR YKKAWLDPEQ GQFLSLNGMW KFKYAPDAAK
     RDTAFVKTTF DVSKWDNIEV PSCWEMKGYD KPVYVNVDYI FADKPPYIKL RNEYKGLVDP
     NPVGSYRRTF TLPTNWDKKN VFLHFDGIYS GAYVWVNGKY IGYTEGGNND AEFDITKAVK
     AGENQVAVQV IRWTDASYLE GQDAFHMSGL HRDVYLVATP QTFVRDHVIT AQLEASKSYT
     AGVMEVNLEL DNRHKLSGKK QIKVSLLDAD NKVVKTATTE VQYTAATEKV MAKVNLDGLT
     NLQPWTAETP YLYNVLVSQQ DEKGNEEMVF NTKYGFRHIE IKQGLVRING KRVFFKGVNT
     QDTHPEKGRT MDVPTMLRDI FLMKQANVNT VRTSHYPRQP KMYAMFDYYG LYIMDEADIE
     CHKNWNDHGA NGGYNTQVIS GRTSWKPMMV DRTERMVLRD RNHPSIVFWS LGNESGAGDN
     FIATYNAARA LDARPIHYEG ATNAGRHTAG LTDINSKMYP DIDFTRRAAN KQGSNTAGQP
     FFMCEYNHAM GNSMGYLREY WDVLESSSVG IGGCIWDWVD QGIYNPQLLK KGERRLTTGY
     DYPGPHQGNF VNNGVITSER EWTPKLTELK KVYQYVRISY NNKTKQLSVT NRYAFRTLQG
     FSLHYSVLRD GESVETGTLD LPALDPQRAH HFPLSLKTAI DNKADYHLNV EMRTTVDEDW
     AKSGYVQAAE QFVLAQRTAL PALPAVKGDV KRLKVDRKNN QVIVSNDRVS MTFDENTAEL
     VAWSYNGQPI LYPGKGAKYD NFRWIENEAP YTSKPYKELG SGHQVPDLFN FGSAPEVTTQ
     QNGQKVIVTA MNEGNVPNPL TYTIHADGTV LLDASFSYNS GKLRRLGVSM GFDRKYNNLD
     YTAKGPQENY VDRQEGSFFG RYKTVVDSNI VNYARTQTCG NRMSLRRLDL TDNEGNGFRV
     ETQGQVDFSI LPYDDHDLVA VEHWWELKKP VYNTAHFDAF QQGLGSGSCG PAETLDKYKA
     FKQDMPMKYT LRFTPLGGLI TGISSPSLSA STAALQLSQP DSSTVVVKGD LTPYHQAQLV
     NLGGVILQSL PLSGSNNLRF SVADLAEGTY LLHLQQTDGT STTLKFFH
//
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