ID A0A1V2QPF0_9PSEU Unreviewed; 934 AA.
AC A0A1V2QPF0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=ALI22I_14160 {ECO:0000313|EMBL:ONI90044.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI90044.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI90044.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI90044.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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}.
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:ONI90044.1}.
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DR EMBL; MTQP01000054; ONI90044.1; -; Genomic_DNA.
DR RefSeq; WP_077005951.1; NZ_MTQP01000054.1.
DR AlphaFoldDB; A0A1V2QPF0; -.
DR STRING; 1933778.ALI22I_14160; -.
DR Proteomes; UP000188617; Unassembled WGS sequence.
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; 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; 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; IPR006311; TAT_signal.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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 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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ONI90044.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188617}.
FT DOMAIN 68..195
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 201..301
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 309..519
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 577..670
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|Pfam:PF16353"
SQ SEQUENCE 934 AA; 102045 MW; B78C33CBEA2253F6 CRC64;
MELNRRNFLE LGAAGLGVAG LSTIGVTAAN AAPAGPGTEV VVLTGTDADH TVDWDFQVTE
GRNSGVWSTI PTPSNWECHG FGTYQWGWNL RPAEKGLYRR GFTAPATWTG KRVFVVFEGS
MTDTEVRVNG TLAGPIHQGG FYRFRYDITS LLRLGQENLL EVTVSRDSTD DSVNNAERRG
DYWNFSGIYR PVSIQAFPAA RIDRIAIDAE ADGSFRADVH LDGVTAAGRV VGQLKRLDGT
NVGAPFSSPV APGTSVATLS TSVASPRTWT AETPHLYRVD VQLTDASGTP LHAVTERFGF
RTIEVRAGDG VYVNGVKVIL KGTNRHTFWP TLGRASSPRL ARMDILLMKE MNNNAVRMSH
YPPDTFFLDL CDELGLYVID ELGGWQKKYD EGVGAPLLAS MVTRDVNHPS ILMWANGNEG
GWNTALDDDY ARYDVQRRPV IHPWDTFGGI NTDHYENYDS TRAILEASNI FMSTEFLHAL
YDGGGGAGLN DYWNLMGSGP RRAGGFIWAF VDEGLVRDDR GGAIDTTGNN APDGVLGPFR
EKEASFYTIR DIWSPVQLAD PDYYATAFPT DFDGTVGVVN RYDFTNLRGC RFTWQLVKHP
SPGATSTDPT VIKHGDVAGP DLAPGGTGKV ALGLPSGWRN ADALRVTAND PDGKALWTWV
WRIKKAADFA KRLVTPTSGA VQVAEDAGSV TMSARGTAIT IDKTTGRLAR VTVHGTAMSL
TNGPAPAAGE ARLTGLTHAR DGRSHVVQAT YSGDLDSVRW RLDPNGWLRL DYRYHRTGEH
DFLGVSLDYP EDKALGLTWL GDGPYRVWKN RLRGVRHGVW SKERNTTATG ATGWEYPEFK
GYHANTYWAA LRTTEGTITL VSEQENLFLR LFTPDVGEDP RFATAPFPTG GISLLDGIPA
MGNKFHAAET LGPEGRKNVA TGEYGRTVHF RFSG
//
