ID A0A401UW17_9CELL Unreviewed; 665 AA.
AC A0A401UW17;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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=CTKZ_04470 {ECO:0000313|EMBL:GCD18885.1};
OS Cellulomonas algicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2071633 {ECO:0000313|EMBL:GCD18885.1, ECO:0000313|Proteomes:UP000288246};
RN [1] {ECO:0000313|EMBL:GCD18885.1, ECO:0000313|Proteomes:UP000288246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKZ-21 {ECO:0000313|EMBL:GCD18885.1,
RC ECO:0000313|Proteomes:UP000288246};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (NOV-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCD18885.1}.
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DR EMBL; BHYL01000034; GCD18885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401UW17; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000288246; 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: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};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084}.
FT DOMAIN 17..388
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 400..601
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 611..662
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 153
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 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 665 AA; 72956 MW; 7FD359B384726FC6 CRC64;
MTNPWPLGVD GIAYGGDYNP EQWPLATRVE DVELMQQAGV TLVSVGIFSW AQLEPRPGEY
DFGWLDDILD RLAAAGIKVA LATATASPPP WLTRKHPELL PELADGTVLH PGGRQAYRVA
APLWREYAVA MTRRMAERYR AHPALALWHV DNELGCHVPH DFSDDAAAAF RRWLESRYGT
VEALNAAWGT AFWSQRYDSF DEVLPPRSAP TYPNPTQQLD FARYSSDELL VHYRALRDVL
REVTPHVPTT TNLMLSTGTK WMDYFSWAGD LDLIANDHYT RAHDPLAHVE LALSADLTRG
VAGGDPWVLM EHSTSAVNWQ PRNRTKRPGE MLRHSLAHVA HGADAVMYFQ WRQSAAGAEK
YHSAMLPHAG TDTDVWRSTV ELGAALKAIG EVKGSRVRSD VAIVWDYPSW WGVELDSHPS
TDVTYPDRVL AHYRALWERH VSVDVVAPSA DLSRYRLVVV PTLYVTSDAD AANIAAAAAA
GATVLVTYFS GIVDEHDHVR LGGYPGAFRD LLGVRTEEFW ALQEGETLTL DDGSVADVWS
ERIHPADGTE VVRTFVDGDL AGGPAVTRRA VGEGSAWYLA TRLDDAALGA LTEALLVEAG
VEPVLSGVPA GVEVARRQAD DGRSWLFVLN HTDAPVDLPP GEVLTGRTSG GQVHAGGYAV
LREQV
//
