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Database: UniProt
Entry: A0A0G3A5A1_9ACTN
LinkDB: A0A0G3A5A1_9ACTN
Original site: A0A0G3A5A1_9ACTN 
ID   A0A0G3A5A1_9ACTN        Unreviewed;      1032 AA.
AC   A0A0G3A5A1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:AKJ09041.1};
GN   ORFNames=ABB07_03065 {ECO:0000313|EMBL:AKJ09041.1};
OS   Streptomyces incarnatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ09041.1, ECO:0000313|Proteomes:UP000035366};
RN   [1] {ECO:0000313|EMBL:AKJ09041.1, ECO:0000313|Proteomes:UP000035366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX   PubMed=26159526;
RA   Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA   Tamura T.;
RT   "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT   the Nucleoside Antibiotic Sinefungin.";
RL   Genome Announc. 3:e00715-e00715(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP011497; AKJ09041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3A5A1; -.
DR   STRING; 665007.ABB07_03065; -.
DR   PATRIC; fig|665007.5.peg.680; -.
DR   Proteomes; UP000035366; Chromosome.
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; PS50022; FA58C_3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1032
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039332451"
FT   DOMAIN          872..1032
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          534..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  110789 MW;  EFD3E8AAA2F11579 CRC64;
     MTVTRRSVLV AATATPAAGA LLSIPAAPAA AAAEASAGTG GRHTVPLRDG WRFALVDPGG
     ITDPTGAYAQ AADPGYDDSA WREVAVPHDW SIEQTPTTDH GTTSGTGFLP GGLGWYRLAF
     TLPPAYAGKR ISVEFDGVYM DSYVYCNGTE AGRHPYGYTG FALDLTGLVH TDGSTPNVLA
     VQVRNQLPSS RWYSGSGIYR EARLVITEPV HVARCGTYIT TLEVSAGSAV VRVATTVLNE
     SGAGTDVRIL SRITGPDGRT VARASSTAAV SDRATETHEL TVGKPLLWDF ATPEHRYTLH
     TELRVAGRTT DNCSTPFGIR TYRFDPEEGF SLNGAYTKIK GVDLHHDQGA LGAAISIDAV
     RRQMRIMKSM GVNAFRTSHN PPSPQMIQVC EELGIVMMVE AFDCWRTGKT KYDYGRFFDE
     WCEKDATEMV LAARNSPAVV LWSIGNEIPD STSTAGLAMA DRIIGAIKAA DDTRPVVIGS
     NKYHGVPAAG SPADLMLAKL DGLGLNYNTA KSVDALHARY PHLFLFESES SSETSTRGAY
     QEPEHLNTGE NHTPGKRETS SYDNNLASWT MSGEYGHKKD RDRKWFAGQF LWSGIDYIGE
     PTPYDVFPVK TSFFGAVDTA GFPKDMYHLF RSQWTSEPMV HLLPMTWNHQ EGDTVEVWAY
     ANVPSVELFL NGKSLGVRRF DVKRTTDGRG YLETTEATGD DKTFTDGPYP GSYTSPTGSA
     GKLHLTWKVP YQPGELKAVA RRDGKVVATD VLRTAGAAHA VRLTADRKSL AADGRSLVFV
     TAEIVDAHGV VVPDAGHLIT FDVGGGSLAG VDNGREESAE RYQASTRTAF HGKALAIVRS
     GTEPGPLTVT ARADGLRTGT ASVSTTPARE TARTPAPIFR PEHPSPPHHP IADASYSGRS
     DTLPAAMLDG DPATGWSNAF AKSPTALLPA FDGARAEDWV SVDFGRARTF DRVAVSFTVD
     STHALPAKAE VAVWDGRTHV PVTGAEVEWA TASDSPTVIT FDAVRGSRLR LTLTSAAPGQ
     AKGAVRISRL EV
//
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