ID U7VBU1_9FUSO Unreviewed; 643 AA.
AC U7VBU1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE Flags: Fragment;
GN ORFNames=HMPREF0202_01848 {ECO:0000313|EMBL:ERT68243.1};
OS Cetobacterium somerae ATCC BAA-474.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Cetobacterium.
OX NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT68243.1, ECO:0000313|Proteomes:UP000017081};
RN [1] {ECO:0000313|EMBL:ERT68243.1, ECO:0000313|Proteomes:UP000017081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT68243.1,
RC ECO:0000313|Proteomes:UP000017081};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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:ERT68243.1}.
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DR EMBL; AXZF01000073; ERT68243.1; -; Genomic_DNA.
DR RefSeq; WP_023051384.1; NZ_KI518221.1.
DR AlphaFoldDB; U7VBU1; -.
DR STRING; 1319815.HMPREF0202_01848; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_0; -.
DR Proteomes; UP000017081; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR013738; Beta_galactosidase_Trimer.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR003476; Glyco_hydro_42.
DR InterPro; IPR013529; Glyco_hydro_42_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR PIRSF; PIRSF001084; B-galactosidase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000017081};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 10..384
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 394..598
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 305
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT NON_TER 643
FT /evidence="ECO:0000313|EMBL:ERT68243.1"
SQ SEQUENCE 643 AA; 75071 MW; 697B6CBC566C0105 CRC64;
MTNKILYGGD YNPEQWLDYP EILKQDIELM KEAKINTITL GMFSWSKLEP KEGVFNFDWL
EDIIKKLSEN KINIILGTPS GAKPTWLGNK YEEVRVVRND GIRELQGNRH NFCTNSPIYR
EKISIINTKL AQISLKYKNI ILWHISNEFG ADCHCELCQQ KFREWLKEKY ENIENLNKMW
WTTFWSHSYE NFDEIHTPMT IGEMSITALD INYRQFMVKN YIDFFNFEKK CIKSITNHLP
FTTNYHGTGN NNMNYREFSK HVDIISYDSY PEWMIKNNLD VAFETAFNFD LMRSTDLNKP
FMLMESSPSS TNWQSYSKLK PNNLLSLASL QSIAHSSLSV LYFQIRQSRG SAEKFHGAII
DHSGKSNHRV FKEVKKLGET LEKLDYKLTN VETKVAIYYS WINKYALERT QGPRNEGMDY
YENVLKVYKS LKSMGVNIDI VFEDSKLDKY KLVIIPMMYV LEKELAEEIK KFVNDGGTIV
TTAPVGYVNN DDLCHLGGFP GYLKEVLGIN IDEIDALTNE EKGEISYKDK LYFSKYFNEM
ITLCNANALG THNKFFYKGQ AAISKNNYGL GSAYHIGTLL EVDGLSDLFE DIFKDLQIEK
AIDNKNLIYN SYLNRHYIFN FTDKLETFKF NNENYVLEPL NYI
//
