GenomeNet

Database: UniProt
Entry: A0A1Q5KN90_9ACTN
LinkDB: A0A1Q5KN90_9ACTN
Original site: A0A1Q5KN90_9ACTN 
ID   A0A1Q5KN90_9ACTN        Unreviewed;       592 AA.
AC   A0A1Q5KN90;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=AMK32_15215 {ECO:0000313|EMBL:OKJ83033.1};
OS   Streptomyces sp. CB01883.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ83033.1, ECO:0000313|Proteomes:UP000186398};
RN   [1] {ECO:0000313|EMBL:OKJ83033.1, ECO:0000313|Proteomes:UP000186398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01883 {ECO:0000313|EMBL:OKJ83033.1,
RC   ECO:0000313|Proteomes:UP000186398};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:OKJ83033.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LIWA01000003; OKJ83033.1; -; Genomic_DNA.
DR   RefSeq; WP_073892754.1; NZ_LIWA01000003.1.
DR   AlphaFoldDB; A0A1Q5KN90; -.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000186398; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186398}.
FT   DOMAIN          11..327
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          376..475
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          514..570
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        156
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   592 AA;  64162 MW;  155E3A777033F03C CRC64;
     MSAFTVGESD FLLDGRPVRL LSGALHYFRV HEEQWGHRLA MLRAMGLNCV ETYVPWNLHE
     PAPGRHRDVG AVGRFLDAVR EAGLWAIVRP GPYICAEWEN GGLPSWVTGG LGARARTRDE
     RFLLHVGSWF RRLLPEIVPR QADRGGPVLM VQVENEYGSY GSDAGYLAEL AALLRAEGVT
     APLFTSDGPE DHMLTGGSLP GVLATVNFGS HAREAFATLR RHRPAGPLMC MEFWCGWFVH
     WAGQHAVRDP GEAAGALREI LECGASVNLY MAHGGTSFGG WAGANRGGDL HEGPLEPDVT
     SYDYDAPVDE YGRPTEKFRR FREVLAEYAD GPLPEPPPRP ASLGAAAEVV LTGWAGLDGV
     LEALGGAETV TPVAPTFEDL RITRGLVRYA VDVPGPRRPY PLTVRGLRDL ATVYVDGEWA
     GVLTEEEPRL PEPVAGPARV ELWVESLGRV NYGPRSGEPK GITGGVLHER QYLHGTRARG
     LDLDAFDDGV ARVPFGPVPD WDTGAVPGAG AAGLYRGTVT VRGAGDARLE LPGWTRGFAW
     INGFGLGRYW SAGPQRSLYV PGPVLREGAN EVWLLELQQA GPDRPAPRLL PV
//
DBGET integrated database retrieval system