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Database: UniProt
Entry: A0A2U1ZXG4_9MICO
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Original site: A0A2U1ZXG4_9MICO 
ID   A0A2U1ZXG4_9MICO        Unreviewed;      1412 AA.
AC   A0A2U1ZXG4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-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=C8046_14515 {ECO:0000313|EMBL:PWD51678.1};
OS   Serinibacter arcticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC   Serinibacter.
OX   NCBI_TaxID=1655435 {ECO:0000313|EMBL:PWD51678.1, ECO:0000313|Proteomes:UP000245166};
RN   [1] {ECO:0000313|EMBL:PWD51678.1, ECO:0000313|Proteomes:UP000245166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCH200 {ECO:0000313|EMBL:PWD51678.1,
RC   ECO:0000313|Proteomes:UP000245166};
RA   Thakur V., Kumar V., Singh D.;
RT   "Genome assembly of novel Miniimonas species PCH200.";
RL   Submitted (MAR-2018) 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   -!- 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:PWD51678.1}.
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DR   EMBL; PYHR01000002; PWD51678.1; -; Genomic_DNA.
DR   OrthoDB; 1095434at2; -.
DR   Proteomes; UP000245166; Unassembled WGS sequence.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.1080; -; 6.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 2.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR038637; NPCBM_sf.
DR   InterPro; IPR001119; SLH_dom.
DR   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF02368; Big_2; 6.
DR   Pfam; PF08305; NPCBM; 2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SMART; SM00635; BID_2; 6.
DR   SMART; SM00776; NPCBM; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 6.
DR   PROSITE; PS51272; SLH; 3.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          1209..1276
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1278..1344
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   DOMAIN          1349..1412
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
SQ   SEQUENCE   1412 AA;  145912 MW;  F01A85B60B5EACEE CRC64;
     MQLDLPWGVE RAPVLDADTE APEVVETDAD VTLTGDDFEL VIDKITGLIT SFVADGEELL
     LEGPTPDFWR PSTQNDVRNS LAARTAPWRE AGRNVAVEEV TITETEAGTV NVQLTGSLPT
     PTSPEYRLGY IVTSDGEVVI RSTMAGESQL AELPAMGTAL VLPGEYDNVT WLGRGPGENW
     NDRNFATTVG LWESTVDEQV YPFPIPQATG HHTDVRWATL TNEAGSGLLV GAVDEPIQFA
     ALPYSEAEIT DTSHHHDLEA DGNVHLAVDG AQQGLGHQWG SPALPKYTLQ SRDAHSFEFL
     LRPITAADDV NALARRTIDL DLLSSITVDG QPIETFHTDV TDYTITFSGA IERDVPVVAA
     APASDGVEIT VTQSEDIPGT ATVTATSADG VSSTTYEIHF EEIQELYLSD IDWLSATIGF
     GTIGRDANLA GQPIRLRAAP GETTYPKGIG THANSSIVYD VSQWDFNRFS TVVGIEQSAS
     SGGRPFQFRI SLDGQVAWTS PSMTKETPGL PVELDIEGVK QVKLDVTFLG ANNGHGHAAW
     ADAKLWSVEE PEEPGEALQL SDIGWQSASS GYLTTSRDQT VDGKPLQVVS SGTDTVTFEK
     GLGVHANSSV VYDLTNRSYA TLAGTAGVGR NASQDGNLFV FSILVDGEEV WSSGQVRRST
     PAKPFELDIA GAARLELRMT AVASNSHGHG VWGSARLEDP IDVAPTAVTV TPGTATLSLG
     ATTTLAAAVA PAEANQAVTW TSSDPTVATV GPNGLVTARK AGTAVVTAAS AVDGAITGTA
     TITVTAIVPT SLTVTPASAS IVAGTTTTLT AQALPAEAVQ AVEWSSSDTS VLTVSPTGVV
     TGREPGTATI TASSLADPSR YAEATVRVTG PVPATVAITP ASSQVVVGAT VTLAATVAPA
     TAEQSVTWSV SDPAVATVSA AGVVSGLRAG TVTVTAASDA DPARRATATV VVRAPAPTAV
     TVTPTATQLE AGATAQLSAS IAPAAADQAV TWRTSDAAVA TVDAAGLVTA LAAGTAEITA
     TSVADGTKAA SATVTVTTQA PPAPTAVTVT PTTTTLEEGD STAIVAAVLP AGAVQTVTWS
     SSDAAVATVD ATGVVTALRA GTATVTATST ADGTRSAGVA VTVTRPAPTS VVVAPTSLDL
     TVGAQAPLTA TVLPAAADQA VTWVSSDETV ATVTAAGVVT ARAAGTATVT ARSVATGVVG
     DVAVTVTEAA SPFLDVASDN LFYAEIVWLF RSNISTGWVD GQGNAEFRPL SPVNRDAMAA
     FLYRLAGSPT FVEPETSPFV DVAKDNLFYK EISWLHAEGI STGWSLPGQP GRSEFRPLAP
     VARDAMAAFL ARFADGVLNR DVEGFDPPAV SPFVDVTTDN LYYREIAWLA HEGISSGWDV
     EGQDGLKEFR PLSSINRDAM AKFMFELMVE AP
//
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