ID A0A0U1NL85_9RHOB Unreviewed; 632 AA.
AC A0A0U1NL85;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=NIG5292_01533 {ECO:0000313|EMBL:CRK75485.1};
OS Nereida ignava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Nereida.
OX NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK75485.1, ECO:0000313|Proteomes:UP000048949};
RN [1] {ECO:0000313|EMBL:CRK75485.1, ECO:0000313|Proteomes:UP000048949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK75485.1,
RC ECO:0000313|Proteomes:UP000048949};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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}.
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DR EMBL; CVQV01000006; CRK75485.1; -; Genomic_DNA.
DR RefSeq; WP_048598906.1; NZ_CVQV01000006.1.
DR AlphaFoldDB; A0A0U1NL85; -.
DR STRING; 282199.GCA_001049735_01532; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000048949; 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: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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:CRK75485.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:CRK75485.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000048949};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 12..396
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 406..591
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 319
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 327
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 632 AA; 71714 MW; 7133EA23ED32E36A CRC64;
MTPIQPRTLG TCYYPEHWDR SIWEDDAQRM VEAGLSWVRI GEFAWSRIEP RESEFHWDWL
DDAIEILGRA GLKVVLGTPT ATPPKWVLNK YPDMLAIDAQ GQPRKFGSRR HYCFSHLPYR
AEAGRITRDL AERYGSNNFI HAWQTDNEYG CHDTVVSYSD AARSGFQNWL AARYGDITAL
NKAWGNVFWS MEYDDFSEID LPNLTVTEPG HIHQLDFMRY SSDMVVAFNK VQTDILRGHT
DAPLIHNYMG RIVEFDHFGV GADLDIASWD SYPIGFLSDR LEASDAHKQH FLRQGDPDFQ
AFHHDLYRAV GRGRMWIMEQ QPGPVNWAPY NPAPLDGMAR LWAWEAFAHG AETVCYFRWR
QAPFAQEQMH AGLLHPDSTD APALSEARQV ANEIKAMPDP KTAKGDVAII FDYASAWAWF
AQPQGADFDY FRLVFDMYRA LRRAGQNVDI LPPDAPSLDG YSAVFAPGLM TIPDGLRKIL
QSTETPIILG PRTDTKDINL TIPTPMGPNV EGLDVTVRIT ESIPPTAKFD LKGGGTARHW
FEHITGDAET YIETIDNQPV LVGSSGLFYL GAWLDEAGFD RVIQMFVTPH KMPAGVRVRD
TDTHRFWFNY NPHSVTIDGN EIPTAGVIWQ KL
//
