ID D2PW47_KRIFD Unreviewed; 972 AA.
AC D2PW47;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Kfla_0583 {ECO:0000313|EMBL:ADB29704.1};
OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB29704.1, ECO:0000313|Proteomes:UP000007967};
RN [1] {ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Kribbella flavida DSM 17836.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB29704.1, ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RX PubMed=21304701;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P., Brettin T.;
RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL Stand. Genomic Sci. 2:186-193(2010).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP001736; ADB29704.1; -; Genomic_DNA.
DR AlphaFoldDB; D2PW47; -.
DR STRING; 479435.Kfla_0583; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; kfl:Kfla_0583; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_11; -.
DR Proteomes; UP000007967; Chromosome.
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; 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; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ADB29704.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADB29704.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007967}.
FT DOMAIN 708..972
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 972 AA; 106378 MW; C63E63844AF85C38 CRC64;
MRYRREVSIS VHQCGFVNRS AVGSMPVTYD HSYVEDFAPG AGVLAPRAWL DDDSARLALT
GDWSFRLSPG LADAPDDLTD PDTSAWDTIS VPGHWQLQGY GAPAYTNVVY PFPLEPPFVP
TDNPTGDYVR AVTVPADWAG ARIVLRFEGV DSRFAVHVDG RLVGWSSGSR LPSEFDLTDL
VAPGKEIRIA VRVHQWSAGS YVEDQDMWWL SGIFREVNLL ALRPSAPTDV FVRAAYDHVD
GAGTLVVESD VPGTVVVPEL GLEVPTGEHV RLDRVEPWSA ESPKLYDGVV RTDGGEVRLR
IGFRTIAIVD GVLTVNGNRV LFNGVNRHEF HPDRGRALTE QDMLDDVLLM KRAGINAVRT
SHYPPHPHFL DLCDLHGLYV VDECDLETHG FGYEPQPPNL PNPVMDERFR DDLVERMRRM
VERDKNHPSI VLWSLGNECG MGDNLRAMYD VAKDRDPSRP VHYERDTQAE FVDVYSQMYT
SLEDVEKIGE DPSSYRGLPF ILCEYGHAMG NGPGGLSDYR ELFERYPRCQ GGFIWEWIDH
GLRTSVDGRQ FFAYGGDFGE TIHDGNFVCD GLLFPDRTPS PGMLEYVKVI EPLVITADGA
GGVSITNRYE VLDTSHLTFE LVTEINGEGV GFGTLPVPAI GPGETTSVQL PPGTIKQREA
NRPETWLTVT ARLTEGTAWA EAGHRVAWGQ LRLDDPAAAD SAAAGPAAGT GSDASVAPGA
VVQGTAGAHG ITVGAISNAR LDVWRAPTDN DAIPGVAEAW KEAGLHRVQH RVVSAGENGS
AWEVVTRTAP PALQWGLIST WRWTRVHDAI QLDLAVRPEG QFPATLPRLG ITFELPKVDS
VEWFGAGPSE AYVDTRAAAA VGKYSASVAQ LQTPYVRPQE NGHRIDTRWA VLTGQETLRI
EAALDLFGLT VRDWTSKDLE DAKHTVDLTA GDTTYVTLDL AQAGIGSNSC GPALPDKYRL
HTAPASLSVR FS
//
