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Database: UniProt
Entry: A0A0D7VXK5_9FLAO
LinkDB: A0A0D7VXK5_9FLAO
Original site: A0A0D7VXK5_9FLAO 
ID   A0A0D7VXK5_9FLAO        Unreviewed;      1047 AA.
AC   A0A0D7VXK5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN   ORFNames=PK35_16175 {ECO:0000313|EMBL:KJD31178.1};
OS   Tamlana nanhaiensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tamlana.
OX   NCBI_TaxID=1382798 {ECO:0000313|EMBL:KJD31178.1, ECO:0000313|Proteomes:UP000032361};
RN   [1] {ECO:0000313|EMBL:KJD31178.1, ECO:0000313|Proteomes:UP000032361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FHC16 {ECO:0000313|EMBL:KJD31178.1,
RC   ECO:0000313|Proteomes:UP000032361};
RX   PubMed=25735434; DOI=10.1007/s10482-015-0410-x;
RA   Liu X., Lai Q., Du Y., Li G., Sun F., Shao Z.;
RT   "Tamlana nanhaiensis sp. nov., isolated from surface seawater collected
RT   from the South China Sea.";
RL   Antonie Van Leeuwenhoek 107:1189-1196(2015).
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:KJD31178.1}.
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DR   EMBL; JTDV01000017; KJD31178.1; -; Genomic_DNA.
DR   RefSeq; WP_044627622.1; NZ_JTDV01000017.1.
DR   AlphaFoldDB; A0A0D7VXK5; -.
DR   STRING; 1382798.PK35_16175; -.
DR   PATRIC; fig|1382798.3.peg.1802; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000032361; 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; 2.70.98.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
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; IPR032312; LacZ_4.
DR   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 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   Pfam; PF16353; LacZ_4; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032361};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1047
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002325075"
FT   DOMAIN          766..1043
FT                   /note="Beta galactosidase small chain/"
FT                   /evidence="ECO:0000259|SMART:SM01038"
SQ   SEQUENCE   1047 AA;  120092 MW;  04ABEAA6BAD30B52 CRC64;
     MRLKSQITAI LLAITASTFA QNTPFWLNEK KNEDNRLPMH ASYLVFENEA VAETDDYTQS
     KNYINLNGTW KFKYVESPSA IPDGFETTSY NDSQWDNFKI PANWDVNGYG YPVYTNTTYD
     FANLIEVNPP NVPTEYNPVG IYRRVFNFDG NTKTNDVLLH VGAAKSNLTV WINGQYVGYG
     EDGKLPQEFL LNPYLKEGEN SIVLKVMKWS DGSYLECQDF WRMSGITRDT YVYSRNKTHL
     VDFEITPDLD ENYQDATLKV STEIKGFSKK SKYTLDVVLK DEDQVIGSKS FSINANTIKN
     TLEFSVSNPK KWTAETPNLY QVHFILKDKK DQVVEVIKTQ TGFRKIEIKG GQLLVNGQPI
     YIKGVNRHET DPTTGQTISR GRMEQDLLML KTYNFNAVRL SHYPNDEYFY QLCDKYGIYV
     VDEANLESHG MGYDITKTLG NKPNWELAHL ERIERMVERD KNHPSIIIWS MGNEAGNGYN
     FYRSYLWLKD RDPSRPIQYE RATVAGWEGA NLKFDWDSDI VDPMYSSPKG MEEYIAANPN
     PSRPFIQCEY AHAMGNSLGN LKDYWDVIRA HKNFQGGFIW DMIDQSVYKT KPDGTKEFAY
     GGDFGPEDVP SDNNFLNNGV FNPEREPNPH AFEAKSVLQE IHTTWANIDK FEVSVFNEFF
     FKNLSNVQLN WELVLDGKPV QNGNITELTN APQETRTYTL NIKEPKKQYQ EAFINISYTL
     KNPEPFIESG VEIAKEQLHF KGTWKNNQSV SPSGSFKVTK TNESISFKSD VTELSFNKTT
     GLLNTYNFQN DSILKPGYTL QPNFWRAPND NDMGAIFQKK LLPWKTVSNA PKLIDFSYKL
     DKNGIVSAKA QYELKDVFAN LTLNYTFNSL GVLNVSQDLQ IEADKETPLL PRFGMKLTLP
     DGFDALNYYG RGPFENYSDR NYSSDVGLYK QTVSEQYYPY IRPQETGNKT DVRWLTLMGK
     NTQLLVTSNA LFSSTALHFL DDDLDDGLEK DQRNASDISE QDLTTLKIDL TQMGVGSIDS
     WGAWPMEKYL LRAKHYNYQF TITPSTK
//
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