ID   F4BNE4_CARS1            Unreviewed;       687 AA.
AC   F4BNE4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN   Name=ganA {ECO:0000313|EMBL:AEB30613.1};
GN   OrderedLocusNames=CAR_c19560 {ECO:0000313|EMBL:AEB30613.1};
OS   Carnobacterium sp. (strain 17-4).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=208596 {ECO:0000313|EMBL:AEB30613.1, ECO:0000313|Proteomes:UP000008304};
RN   [1] {ECO:0000313|EMBL:AEB30613.1, ECO:0000313|Proteomes:UP000008304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17-4 {ECO:0000313|EMBL:AEB30613.1,
RC   ECO:0000313|Proteomes:UP000008304};
RX   PubMed=21551290; DOI=10.1128/JB.05113-11;
RA   Voget S., Klippel B., Daniel R., Antranikian G.;
RT   "Complete gnome sequence of Carnobacterium sp. 17-4.";
RL   J. Bacteriol. 193:3403-3404(2011).
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         ECO:0000256|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR   EMBL; CP002563; AEB30613.1; -; Genomic_DNA.
DR   RefSeq; WP_013711555.1; NC_015391.1.
DR   AlphaFoldDB; F4BNE4; -.
DR   STRING; 208596.CAR_c19560; -.
DR   KEGG; crn:CAR_c19560; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_9; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000008304; Chromosome.
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:0006012; P:galactose 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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
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; IPR013780; Glyco_hydro_b.
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; PF08533; Glyco_hydro_42C; 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.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:AEB30613.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:AEB30613.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008304};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          20..401
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          411..616
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          627..683
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        158
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        322
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   687 AA;  79325 MW;  F1541BB224768C0F CRC64;
     MNERKKKQVT KANFLLHGGD YNPDQWLDCP DILAEDLSLM KLANTNTYSI GIFAWSALEP
     EEDSYTFEWM DKIIEDIHQN GGNIILATPS GARPAWMSEK YPEVLRVNEN RQKQLQGARH
     NHCFSSKVYR EKTQKMNRKL AERYGDHPAL IMWHISNEYG GECHCDLCQE AFREWLKKEY
     NADLKALNDA WWGPFWSHTF TSWSQIQSPS PIGENAVHGL NLDWHRFVTD QTIDFYENEI
     VPMRELTPEI PITTNFMADT TDLIPFQSLD YSKFAKHVDV ISWDAYPAWH NDWESTAELA
     SKVAFIDDLY RSLKQQPFIL MESTPSGVNW HPVNKAKRPG MHLLSSMQML AHGSDSIMYF
     QWRKSRGSSE KFHGAVVDHD KSPENRVFKD VSDVGAVLKK LDNVVGSTRS AEVAFLYDWE
     SNWALDHAQG FGLETKQYPQ TIQKQYRSFW EKDIAVDVIT KEQDFSAYRL LVVPMLYLMS
     EETINQLKSF VSNGGVLVSG YMTGLVDEHD LAYLGGWPEQ LQEIFGMKPL ETDTLYPKDK
     NEIQYKGKNY LLKEYATIIE VEDATVIGTY QEDFYAHTPA ITKHAYGKGE SYYIGGRLEH
     SFYEDFYGQL IEELNLKPKL FIQHDKGVSV QTRQTEEEDI TFVMNFSEEE QKIVLTETVK
     DSLNDTILSG EVILDPYGFK VLSKKIK
//