ID A0A1G0Y6U9_9BACT Unreviewed; 1714 AA.
AC A0A1G0Y6U9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2X48_13500 {ECO:0000313|EMBL:OGV41629.1};
OS Lentisphaerae bacterium GWF2_49_21.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798573 {ECO:0000313|EMBL:OGV41629.1, ECO:0000313|Proteomes:UP000178513};
RN [1] {ECO:0000313|EMBL:OGV41629.1, ECO:0000313|Proteomes:UP000178513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV41629.1}.
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DR EMBL; MHBH01000026; OGV41629.1; -; Genomic_DNA.
DR STRING; 1798573.A2X48_13500; -.
DR Proteomes; UP000178513; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1190; -; 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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1714
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009570056"
FT DOMAIN 642..741
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 785..902
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 1714 AA; 189289 MW; E553B4FEFBF436F5 CRC64;
MLKTKFACLL MFSMTLLSST SVFSAEKELP DGRIDIDVKN GPADLNLSVV EASEDTKASN
ASKTGLNWYF PTDDRAWSQS TLKIKSNMDC KARLRLKSKF TKPEEAVWVL YDGIQVEGAE
LRNADLEDQP DSKRNGWIFE EQVPGLGPKF IKEEGVAKSG KGCFLVWHNG PATYNGFNLP
ANKVVTISVW AKKPPKDMIP GAGGAADVQT VAKFASDPIS LASVANMGFK DEVTNDDAGG
WTDEGPNNDI SCMTPGRKVL RDVTFEILDP AANNGKGCIV MSAPNLKNGT WTQKAITHKY
GGKLKTQTDN VEIPAGDKAY KFVYLLHAMG WAPDEKRTIG TITAKYADGS STEIPVQATV
DVSNWWNPQA MQNGFPAWKG RNLKAEIGLY LSKFPVDDKP LKSLKFECKD CAWMIMGVSA
SRDNIPMPVF APPSFDFTQE SLAKRYPAFS AAADIATAMK SEKALETKFG LLDGRPTAWL
HGEWNIIPVM EKNAAVKGKE ITSSKVFVPS FLGSSKGTLK KAAYAPQPES WQKATVFWYS
TNVAVPQEFT GGPLVVHFDA VDFLGAVFIN GEFQKIHTGR FTPFNVYLPD SIKPGDTFNL
SVFCLKLAEG VLNQACPFMQ GVSPDVGGIT APVYLFRDTP LKIENLRIVT SLTGKKLSVS
FKCSGNVTGA TVEPKVVDAS GTPVALAGLA TKPAAAEMSW ETAWDNPHLW SDEDPYLYRL
QMTVKSAEGK ETVQEQTFGF REISIKGGDI VLNGSPVRLF GLSYEPQCLD AWPRTDEEFN
YKYLMALKKH FGVNAVRFHH IPAWPAQLRA ADRAGILAIN QSGLWTGGRF ANYRAGNLFI
ETMKKELSEW VWRDINHPST IIWDTANEYI IGSPEWHDFW VKLDEIVKDI DKTRPVEQSG
SGFEYRNPMI RHFHNRENYD QVFDFMKKKE TPSIFGEFWI GSGKRILTLP RTTFTVEGFN
REWVRCLEDK MTLMRVNGGA GFFPFHQIEH GLEMLGQDVP KNAKFAISSF NPVKMDDRYE
INTFKPSDKQ VNPIFVEACN RFYGKVAGLW FERSQVFSKK VKTERNLFLA NDTRSEKKYD
VSITLKIGSE EMPVAKFAET LAAGQTMTRK IEVPGAKTAG QGLLIVKISY GGEKEFVNET
PAQVVDDASY GQALTVRLYK GSEALQSVLK AAGITVQAVD KLEAGTSPLL IGEDTLGFGD
KSQMEALMRT GDQKILVLAQ SKVSFADILG LGYVTPSPTE TSSYSSAQNK KLIASGISSY
DYPGGIGRSY FGTYIMPMPA EQIPPSIEKL FTGTRFEDVP CLRYEMAKGN AIFCQLQLEK
HFLDDARAKK ILLELARLLD EKSARNPGAV YTKSDEIKET LGTFGFKVAE KPDDAKLAVV
SHKEYKADPK LQQMKDVVVY ALEENGEIDG KKIATKMVRH FTTFMVSAEV PGLYEMGTAN
FTKIMEAGGF CKAVNPPTLP SINIPDSKIA AAGKKASMHY DIFDDDNYNP VIRYYEIDGK
RRWVTGFDDT WNPTAAIGLC VAKDMGMEFR RELGALTYSI VDAREVKIDG NVEDWTYDGD
INLRNWARAN PLIVGNANPW GIFYMMADSA NLYVAFAAPE DSLPVGNANA KLVLKMDKNE
LVIKRQADGA LNVALDGAVL ADPAKWLPVT ATLVDAGARQ DEMNKGFTLE ISIPLAKLAL
QKRMAGSIEL NDGKAQVTVP AAGAGSKTFK LVME
//
