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Database: UniProt
Entry: A0A1H5UV91_9ACTN
LinkDB: A0A1H5UV91_9ACTN
Original site: A0A1H5UV91_9ACTN 
ID   A0A1H5UV91_9ACTN        Unreviewed;       957 AA.
AC   A0A1H5UV91;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=SAMN05444920_101663 {ECO:0000313|EMBL:SEF78926.1};
OS   Nonomuraea solani.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEF78926.1, ECO:0000313|Proteomes:UP000236732};
RN   [1] {ECO:0000313|EMBL:SEF78926.1, ECO:0000313|Proteomes:UP000236732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEF78926.1,
RC   ECO:0000313|Proteomes:UP000236732};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNVT01000001; SEF78926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5UV91; -.
DR   Proteomes; UP000236732; 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; 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; 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:UP000236732};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           44..957
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009286593"
FT   DOMAIN          386..562
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
FT   REGION          737..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  103732 MW;  008A97944262954A CRC64;
     MVAKLKGRVP FRADPWKATM RRLFPVLLAL LLTCVAVPGQ ARAAGEVTYD EHSLMVDGRR
     IVLQSAEFHY FRLPSQELWE DVLEKFKAAG FNAVSLYFSW AYHSPRPGVY DFTGVRDVDR
     LLRTAERAGL YVIARPGPYI NAESTGGGFP AWLKTVPGRA RSFEAGYREA YREWLHRINP
     IIARHQVTEG GPVILYNAEN EYQVNTDAAY MQDIQDQARA DGIEVPITTN DCCDAGSWSS
     TWATGPGAVQ IPGVDDYPQS FECANPELWG PWGEGLTEKL RDDIPVFAAE YQAGAIDLGN
     AGYERCRELT GPAFMKFFYK NNLMRTGATM FSYYMGYGGT NWGWLAQPND VYTSYDYGAA
     ITEARQLTPK YDEFKRQGLF LQAVTPLAKT GAVPSPATSG NAALTTVARA NPDTGTQFVL
     VRHEDRAATS TDETILDWAA PDGRHQVPVQ VKGRDAHVLV AGYDLGGQRL AVSSSEIMTH
     AAIGGRDVAV LYGTAGSPGA TVLRYASRPT VKVLEGRVRV TYDEGDLRLD YAHEGLARVL
     VTGGGRRPLL LLIGTDETAA EFWRAETAAG PVLVRGTELV RSATSYGDTV RLAADTKAGP
     VEVFTPADRL RIGQDEIRVT RTPSGSLLGA TRAPGQAHLP ALTGWRAHAE SPEAAPGFDD
     SRWTAADHTT TVSPHKPKTL PVLYADDYGF HYGNVWYRGH FTATGSETRV DLNAITGLRG
     NYLVWLNGRY LGSAAGGVQA DSGDQATPPN PDPGPGRFDI PDGLLKAGAG NVLSVLVATT
     GHNDDWIADD LRFKQPRGLV AASVGDTPIT WRIQGTAGTD RLRGPLSTGG LYGERTGWHL
     PTYPDKSWNS ATGTLPPGVT WQRTSFRLDL PKGQDVPVGL RFGGDPSPAY RVLIFLNGWN
     IGQYGADIGP QREFSLPAGL LNEHGTNTLA LAITAEQPTT GPGPLGLFAY GNVRSGR
//
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