ID Q9ZBD1_9PSEU Unreviewed; 1251 AA.
AC Q9ZBD1;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 100.
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};
OS Saccharopolyspora rectivirgula.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=28042 {ECO:0000313|EMBL:BAA34817.1};
RN [1] {ECO:0000313|EMBL:BAA34817.1}
RP NUCLEOTIDE SEQUENCE.
RA Ochiai M.I.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAA34817.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9774708; DOI=10.1016/S0167-4838(98)00187-3;
RA Inohara-Ochiai M., Nakayama T., Nakao M., Fujita T., Ueda T., Ashikari T.,
RA Nishino T., Shibano Y.;
RT "Unique primary structure of a thermostable multimetal beta-galactosidase
RT from Saccharopolyspora rectivirgula.";
RL Biochim. Biophys. Acta 1388:77-83(1998).
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; D86429; BAA34817.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZBD1; -.
DR SMR; Q9ZBD1; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
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; 2.60.120.200; -; 1.
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; IPR013320; ConA-like_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; 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; IPR006558; LamG-like.
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; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1251
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004337367"
FT DOMAIN 655..790
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 972..1248
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 941..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1251 AA; 139979 MW; 825C3E825AF6D6AF CRC64;
MRRRMHPAVL LATLAVTAGL LLPAAHAQPV DGPSDPAEIE SYLEDPQRTG EGQQPPHAFL
RPYADAEQAL RSAREDLFAP ADEPTPWTLS LNGRWQFQYA DHYRDLPAGW QRGSGEWDAV
DVPGVWQQQG YDRPIYRNVS SEIAPYRPPE VPDDINPTGA YRKQFELPEH WAGRRQLLRF
EGVTSGYFVW VNGHYVGYDQ GGYTPAEFDV TPHLRPGTNT IAVQVHRWSS GSYLENMDFW
HFSGIFREVH LYSVPRTHLE DVTVRTELDD TYTDATLRLG AELRHLPGGT TGRHELRATL
YDPDGNRVAE VSEPVVVDRE TASAELAQHV AAPRLWSDET PHLYTAVLEL LHNGQVVHTT
QQPVGFRSVE VRDEQLLLNG KPVELRGVNR HEHDPRTGRA VSRQRQQQDV ELLRQHNINA
VRTSHYPNDP YWYRLADHHG ILLADEVDVE THYREDCSNP ADDCLADRPE WQAAFADRFH
ALLERDKNHP SVIIWDTGNE AGLGAAHYAM AEHARATDPT RPLYHQSNSP DGDAPYADIW
GPRYPSPQRL EEIADETTKP VVMGEWLHAM GNSLGHYEDM WRTIRREPAL QGGFVWDWVD
QGLYRPLRTT PANIPVHYGG NPRPVPGVSG NGLLLSGLDD WVEAYRDPAL DITGRQVTLD
MWVKPLSWQG SGTFLSKGDK QWALQMPDPE HVEFFVYGED DWHTARVRIP DDWWGNWHRL
SGVYDGEQVR LHLDGEQVAA TPYRGEIAAN TMYTASIGRN QEKHGDSFAG RTAHAVVDSV
RVYDTALTRQ QLEDDPAERA VLALDFETEQ QNGEFLDYGS SNFVVNGLVN ADRTPQPELA
QLAYSHAPVR FEGTGEPGEF RVHNRNHTLT TEAYDLTWRL VEGGRDIASG ALDVVVGPGQ
QQLVELDLPP AGGTQRYLVL EARQRADAPG VPRGHLVATE QLPAGGTQPP PPPESGGEPQ
PLAVHEHGNA VEVSAPDFTY TFDREAGTLT GMTANGQQHL VRGPQLDVFR APIGNEWSDW
SGLAPEAQFR AVGLDRLRTE VTDFTVSQPA PDQVRVSVRT DVSAPDVPDD GFRSTWVYTV
DGTGAITIDH QVDAYGERMR ALPWLPRVGM SMAVPDSFGQ LDWYGRGPGE SYPDRKDAQH
IGRWSQTVDE SWFDFLPPQD NGVKTDTWWA VLSGDRGGLQ VSGDRLAIAA DRFSNAERTD
FAHQLRRDDF VTLHVSAAVT GLGDTPVPVQ PEYRVAPDQQ HSYSVTLRPV P
//
