ID   A0A1C4QJ72_9ACTN        Unreviewed;      1075 AA.
AC   A0A1C4QJ72;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:SCE22751.1};
GN   ORFNames=GA0115240_144869 {ECO:0000313|EMBL:SCE22751.1};
OS   Streptomyces sp. DvalAA-14.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839759 {ECO:0000313|EMBL:SCE22751.1, ECO:0000313|Proteomes:UP000199020};
RN   [1] {ECO:0000313|EMBL:SCE22751.1, ECO:0000313|Proteomes:UP000199020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DvalAA-14 {ECO:0000313|EMBL:SCE22751.1,
RC   ECO:0000313|Proteomes:UP000199020};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FMCH01000413; SCE22751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4QJ72; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000199020; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
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; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 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   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199020}.
FT   DOMAIN          83..215
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          259..357
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          364..518
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          690..786
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          800..899
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
FT   DOMAIN          934..1058
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
FT   REGION          27..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1075 AA;  114309 MW;  434A9E6AE67D0E45 CRC64;
     MPVNRRSILI AGAAGAAAAP ALPGLTGVAS AHSAPPSSSS PTSSAPTKTP IPRTVDLADG
     WRFVLVNPAG ITDPTGAYAN AADPDFDDSR WRAVRVPHDW SIEQTPGTDN GTSGGTGYLP
     GGLGWYRKAF TLPPTVAGRR VSVEFDGVYM DSYIYCNGTL VGNHPYGYTG FAFDLTDLLH
     TDGRTPNVIA VEVRNQLPSS RWYSGSGIYR NARLVITDPV HVARWGTYVT TPGLADTVQA
     GDGGKAGNAG NARGGGRDDH GYATVRAQIG LVNESAAATS VTVLNTVRDH DNRQVAQARS
     QLDLPAGATA QEVTVEMRVD RPALWSFDTP ENRYRLDTEV QVHGRTVDTY STDFGMRYIT
     LDPDQGLFVN GEHAKIQGVD LHHDQGALGS AINADAVLRQ MTIMKSMGVN AFRTSHNPPS
     PQMIRVCEDL GIVMMVEAFD CWHNGKNTYD YGRFFDANSA SDIAEMVGAA RNSPAVMMWS
     IGNEIPDSTS TAGLAMADGL ITAIRALDTS RPIVIGSDKY RGLPAVGSAA DLMLAKLDGL
     GLNYNTAASV DALHARYPHL FLFESESSSE TSSRGTYQEP DHLNTGENYT PGKRAASSYD
     NNLASWTMSG EYGLKKDRDR AFFAGEFLWS GTDYIGEPTP YGVFPVKASF FGAVDTAGFP
     KDMYHLFRSQ WTSEPMVHLL PMDWTDHKPG DVVEVWAYSN VETVELFLNG RSLGVRNFDV
     KKTLDGRTYL ETTEATFDDK TVTDGPFPGS YTSPNGSAGK LHLTWNVPFA AGELKAVARR
     HGRTVATDIL RTAGDPHTVR LTPDRNSLVA DGTSLVYVTA EVIDARGVVV PGADHLITFK
     AAGGSLAGLD NGQQESAERY QATTRTAFHG KALAIVRSGT DAGHLTVSAT APGLHPGSTS
     VRTTRASGAV ASTPPARFAP DPGPGAPVYP LADASYSGAT TSVPAAMLDG NPATGWSNAF
     KKSATALLPA FSGARPADWV SVTWATAQTI TTLSVTFTID ATHSLPATIT VSYLDGDRWI
     PVRRPVITWA TTTGTPTVIT FSGVHTAAVR LDMTSAAPDT AAGAQRITEL SAGAV
//