ID A0A2Z2NVX5_9GAMM Unreviewed; 684 AA.
AC A0A2Z2NVX5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=IMCC3135_27815 {ECO:0000313|EMBL:ASJ75616.1};
OS Granulosicoccus antarcticus IMCC3135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Granulosicoccaceae; Granulosicoccus.
OX NCBI_TaxID=1192854 {ECO:0000313|EMBL:ASJ75616.1, ECO:0000313|Proteomes:UP000250079};
RN [1] {ECO:0000313|EMBL:ASJ75616.1, ECO:0000313|Proteomes:UP000250079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3135 {ECO:0000313|EMBL:ASJ75616.1,
RC ECO:0000313|Proteomes:UP000250079};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
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DR EMBL; CP018632; ASJ75616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2NVX5; -.
DR KEGG; gai:IMCC3135_27815; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000250079; 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: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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ASJ75616.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ASJ75616.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000250079};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 6..390
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 424..574
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 684 AA; 76967 MW; 0D5D2FCE4F9DD41F CRC64;
MKTGVCYYPE HWPEEQWAHD AAHMRKLGLS VIRIGEFAWS RLETQDGKLH LDWLERAIDT
LHEAGLSVVL GTPTATPPRW MLDRHPDMLA VDADGRIRDF GSRRHYCFSH EPYLDECRRI
VTLLAERFGQ HPAIMAWQTD NEYGCHSTSI SYSPHALAAF QRWCATQYAD VEALNLAWGN
VFWSMEYDNF EQIGLPVGTV TESNPAHQLA FWRFSSDQIK RFNRAQVDII RKHSPGRDVL
HNFMGNFVEF DHHDVSTDLD IATWDNYPLG FLTRDNGDAD DQQAFLRTGH PDGSAFHHDL
YRGCCNGRWW VMEQQPGPVN WAPYNPSPVD GMVRLWGWEA YAHGAEVMSY FRWRQAPFAQ
EQTHTGLLLS NGDADVAASE VATLNRELAE VAAFDVGELM RSDTPVSESP NVAESLKSLP
VHSDVAIVFS YAGIAIQDIQ LPGGSSYSPL GFCQRVHSAC RQWGVNVDIV SPAASLDQYR
LVLVCTSTED EDDLVKRLQS AHKQHQAVIA LFPGTGSRSH DYTMPDNLPP GYFQQLLPLQ
IIRSESLPAE QSMTATDSHG LSRSCSQWRE RIASSIEPRM SFGDGWGFHY EQDHIHYINA
IPEKNALIPM IGELLVEAGI PCRELGAYLR TQRIGPYQLA FNFGKQAVEL DKALGTVLNF
HHDTPLLVGS RTLGQAEVAV WVAG
//
