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Database: UniProt
Entry: A0A438LYF2_9ACTN
LinkDB: A0A438LYF2_9ACTN
Original site: A0A438LYF2_9ACTN 
ID   A0A438LYF2_9ACTN        Unreviewed;       935 AA.
AC   A0A438LYF2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=EDD27_0803 {ECO:0000313|EMBL:RVX38491.1};
OS   Nonomuraea polychroma.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX38491.1, ECO:0000313|Proteomes:UP000284824};
RN   [1] {ECO:0000313|EMBL:RVX38491.1, ECO:0000313|Proteomes:UP000284824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX38491.1,
RC   ECO:0000313|Proteomes:UP000284824};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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 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:RVX38491.1}.
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DR   EMBL; SAUN01000001; RVX38491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A438LYF2; -.
DR   Proteomes; UP000284824; 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; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
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; PF13364; BetaGal_ABD2; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284824};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..935
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019288098"
FT   DOMAIN          363..534
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
SQ   SEQUENCE   935 AA;  100291 MW;  076F7CD43F514412 CRC64;
     MLLAMLLTCA ALVAPARAAA AREVTYDRYS LMVDGRRVVL QAAEFHYFRL PSPRLWRDVL
     EKFKAAGFNA VSLYFSWAYH SPKSGVYDFT GVRDVDRLLR MASEAGLYVI ARPGPYINAE
     SSGGGLPAWV KTVPGRARSS ESGYQAAYRE WLHHINPIIA RHQITGGGPV ILYNAENEYQ
     VNTDAAYMQD IQDQARADGI DVPITTNDCC DGGSWSSTWA TGPGAVQIPG IDDYPQSFEC
     ANPGLWGPWG EGLTERLRDD IPVFAAEYQA GAIDVGNAGY DKCRELTGPA FMKYFYKNNL
     VTTGATMFSY YMGYGGTNWG WLAQPNDVYT SYDYGAPITE ARRLTPKYDE FKRQGYFLQA
     VTPLAKTDPL AAPPVDNPAL TTVARANPDT GTQFVLVKHA DRAATSTDAA TLDWAGHRVP
     VQVKGRDAHV LVAGYDLGAQ RLTLSTSELM THAAIGGRDV AVLYGTSGSP GATILRYGSE
     PRVTVLDGRV TSTYSGGDLR LDYTHEGLAR VLVTGGGRRP LLLLIGTDAE AASFWRTDTA
     SGPVLVRGTD LVRAASVNDG TVRLTADVAA AGEVEVFAPP AAHRLRIGAD DVRVTRTSSG
     SLLGSTRPPG PAPLPALTGW RAHAESPEAQ PGFDDSRWTV ADRTTTTSPH PPKTLPVLYA
     DDYGYHYGNV WYRGHFTATG AETTIDLNAV TGLRGNYLVW LNGRYLGSAA GGVQADSGDQ
     WTPPNPDPGP GHFAIPSGLL KPGADNVIAV LVANMGHNDD WIADDLRFKQ PRGLVGASAG
     GTPISWRIQG AAGVDPVRGG LNNGGLYGER TGWHLPTYPD KSWKPANPAA TPLPPGVTWY
     RTSFRLDLPA NQDVPVGLRF GGEPSPAYLV QIFLNGWNVG QYGGDIGPQR EFSVPAGLLN
     EHGTNTLALA VTAEQPVPAG PGPISLFAYG NVRVD
//
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