ID A6WF44_KINRD Unreviewed; 678 AA.
AC A6WF44;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
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 OrderedLocusNames=Krad_3970 {ECO:0000313|EMBL:ABS05433.1};
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS05433.1, ECO:0000313|Proteomes:UP000001116};
RN [1] {ECO:0000313|Proteomes:UP000001116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC {ECO:0000313|Proteomes:UP000001116};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA Fliermans C., Richardson P.;
RT "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL Submitted (JUL-2007) 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; CP000750; ABS05433.1; -; Genomic_DNA.
DR RefSeq; WP_012086281.1; NC_009664.2.
DR AlphaFoldDB; A6WF44; -.
DR STRING; 266940.Krad_3970; -.
DR CAZy; GH42; Glycoside Hydrolase Family 42.
DR KEGG; kra:Krad_3970; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_11; -.
DR Proteomes; UP000001116; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ABS05433.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ABS05433.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 16..386
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 400..609
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 622..673
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 152
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 678 AA; 73370 MW; DB0376970619D877 CRC64;
MQRWSDGAAG LVFGSDYNPE QWPAEVRADD VRLMQRAGVN LVSVGIFSWG LLEPRPGRFD
FGWFDAVLDD LHAGGIGVSL ATATASPPAW LGELHPEVLP VDADGHRVVF GSRQSWCPSS
PVYRERSLAL VEALAERYGQ HPALRLWHVS NELGCHNARC YCDVSAAAFR TWLADRYPDV
AALNDAWATA FWSQHYTSFE QVQVPARTSS FHNPAQALDF ARFSSDELLG QHLAEKDVLR
RVTPEVPVTT NFMIGSQLNP MDYGRWAREQ DVVANDHYLI HGNYDDPRAE LAYSADLTRG
TASGQPWLLM EHSTSAVNWQ PVNVAKPAGE MLQDSLSHVA RGADGICFFQ WRASAGGAEQ
WHSALVPHAG EDTERFREVT ELGALLGRLG ELRGSTTSND VAILVDWQNA WAMESETLPS
RRVGHADLAL RVHGLLREAR TGADVVPVGA HPHDLAEVLA GYRVLVVPTL YLCDDTTAAA
VTAAAESGTH VLVTYFSGIV DETARVRLGG YPGAFRDLLG IRVEEFHPLP DGVAGELDDA
TVGDVWSEIA TADDDVEVLS RYAEGATAGC PALTRRDLPS GARAWYLGTS LDDEALAGLL
HAVCTTAGVA PVAEASGPVD VVRRRAADGR SWLFALNHGE EPATVTVRGF DLVAEVDVDG
LDLEPGASAV VRELGPGD
//
