ID A0A1G8X0U0_9ACTN Unreviewed; 925 AA.
AC A0A1G8X0U0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05421874_103366 {ECO:0000313|EMBL:SDJ84232.1};
OS Nonomuraea maritima.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=683260 {ECO:0000313|EMBL:SDJ84232.1, ECO:0000313|Proteomes:UP000198683};
RN [1] {ECO:0000313|EMBL:SDJ84232.1, ECO:0000313|Proteomes:UP000198683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDJ84232.1,
RC ECO:0000313|Proteomes:UP000198683};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; FNFB01000003; SDJ84232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8X0U0; -.
DR STRING; 683260.SAMN05421874_103366; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000198683; 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; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000198683}.
FT DOMAIN 668..923
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 925 AA; 102278 MW; 22955ED484AA559F CRC64;
MDLETFTPGS GRLEPRAALR SDAPALDLNG TWRFRLSPTA DVPADFADPG YDDSSWDDLP
VPAHWVLHGH GAPAYTNVRY PIPVDPPHVP NENPTGDHRR VFDLPDGWTG GRLRFEGSDS
FTRVWLNGHE LGFSTGSRLP VEYDAGPHLR PGRNVLAVRV HQWSAATYLE DQDMWWLPGI
FRDVTLTRSS ADVFVHAAYQ DGRGRLSFDG SGTLSVPELG VTGLRPGEEV TLDVEPWTAE
TPRLYDAELT LPEETVRLRV GFRTISIEDG VLLANGRPLL LKGVNRHEFH PEHGRAVPYE
TMREDVLLMK RHNVNAVRTS HYPPHPAFLD LCDELGLWVI DECDLETHGF GEVGWRGNPT
DDPRYADALL DRMRRMVERD KNHPSVIMWS LGNEAGVGRN LAVMADWTRE RDPSRPLHYE
GDRSCAHTDV YSRMYATHAE VEAIGRGEED PLDDAELDAR RRRMPFLQCE YAHAMGNGPG
GLAEYQELFE RYPRLAGGFV WEWIDHGLVH PELGYAYGGD YGEPLHDGNF VIDGLVFPDR
TPSPGLLDLK KVFEPVRFAF GDGFVRVVNG HGFADLSHLE FVATVTVEGA TVAEHRLEVP
AAGGECKLPD LTGGPDGERW LTVRAVLAGD LPWAPAGHEV AWGQTRLAGP ATPSRGPAGP
AFVRDGGELT AGGCAFDAAT GRLTRLFGLD VEGPRLDLWR APTDNDRYGG LEGRWRALGL
HRLTHRVDDV ATGDGLTVRT RVAPAATDLG MWATYRWTFD GGLRLELDIE PDGEWPDPIP
AIGVTMSLPG DAVERVTWFG QGPGEAYQDT GLATRIGRWS ATVEELQIPY VMPQENGRRA
GVRWADLGAF RVSGEPEYGL SVRRWSTDEL AEARHLPDLV PGERVHLHLD LAQQGIGTAT
CGPGPLPVYD LMARPATLRL RFDPS
//
