ID A0A1H0R0G4_9BURK Unreviewed; 650 AA.
AC A0A1H0R0G4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=SAMN05216303_103429 {ECO:0000313|EMBL:SDP23033.1};
OS Rhodoferax sp. OV413.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1855285 {ECO:0000313|EMBL:SDP23033.1, ECO:0000313|Proteomes:UP000199151};
RN [1] {ECO:0000313|Proteomes:UP000199151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV413 {ECO:0000313|Proteomes:UP000199151};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 ECO:0000256|PIRNR:PIRNR001084};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNJA01000003; SDP23033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0R0G4; -.
DR STRING; 1855285.SAMN05216303_103429; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000199151; 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 Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000199151};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 6..391
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 402..595
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 650 AA; 72760 MW; 88D0AD113BE4EAA4 CRC64;
MKLGVCYYPE HWPESWWPDD ARRMVEVGIQ YVRIAEFAWS RIEPSPGVFA WEWLDRAIAT
LHAAGLKVVM CTPTATPPKW LVDADPGMLA VDAHGQTRGF GSRRHYCFSS LSYRAQSARI
TTALGERYGQ HPAVVAWQTD NEYGCHDTVV SYSAAARQGF RAWLQQRYSD ITALNTAWGT
VFWSQEYRNF EEVDAPVGTV TEVTPAQRLD YQRFASDEVV AFNRIQVDIL RQHSPGRDVV
HNFMGFFTEF DHHTLSADLD VATWDSYPLG FTQNFFLTPE EKRHYARIGH PDIASFHHDL
YRGMCKGRWW VMEQQPGPVN WAQWNPAPLD GMVRLWTWQA FAHGAEVVSY FRWRQAPFAQ
EQMHAGLNRP DRTLDQGGLE ATQVAQELRQ LQAHLPTTYQ QAPVALVFDF TSIWMAKIQP
QGADFNAVEL SFRAYSMLRQ MGLDVDIVSS SADLDGYALV VLPAHLREDT ALAARLARSK
AQVVLGPRSG SKSEALAFPG NMPPGAFAEL AGVTVQRVAS LPPGLVDSVH WNDGGHTEAS
RWREDLACTT AAPVAVFADN RPAVTHNGST WYTAGWLDAA GWRRVLGLAA QAAQLTVQDL
PPDVRTRRCG DLQFVMNFSG SEVQFAPATH AQCLLGARDL APQAVSIWKL
//
