ID A0A098S1L8_9BACT Unreviewed; 381 AA.
AC A0A098S1L8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=IX84_22790 {ECO:0000313|EMBL:KGE86249.1};
OS Phaeodactylibacter xiamenensis.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC Phaeodactylibacter.
OX NCBI_TaxID=1524460 {ECO:0000313|EMBL:KGE86249.1, ECO:0000313|Proteomes:UP000029736};
RN [1] {ECO:0000313|EMBL:KGE86249.1, ECO:0000313|Proteomes:UP000029736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD52 {ECO:0000313|EMBL:KGE86249.1,
RC ECO:0000313|Proteomes:UP000029736};
RX PubMed=25052393; DOI=10.1099/ijs.0.063909-0;
RA Chen Z.Jr., Lei X., Lai Q., Li Y., Zhang B., Zhang J., Zhang H., Yang L.,
RA Zheng W., Tian Y., Yu Z., Xu H.Jr., Zheng T.;
RT "Phaeodactylibacter xiamenensis gen. nov., sp. nov., a member of the family
RT Saprospiraceae isolated from the marine alga Phaeodactylum tricornutum.";
RL Int. J. Syst. Evol. Microbiol. 64:3496-3502(2014).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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:KGE86249.1}.
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DR EMBL; JPOS01000081; KGE86249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098S1L8; -.
DR STRING; 1524460.IX84_22790; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000029736; 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 PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 1.
DR Pfam; PF08532; Glyco_hydro_42M; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029736}.
FT DOMAIN 25..87
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 100..313
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 340..380
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
SQ SEQUENCE 381 AA; 42593 MW; CE22F4EB2623575B CRC64;
MHWLFETAPN NSGGGAKGNT WFLHQPDGSM HTALWMNYAL GGQGAIFWLW RQHRAGQEMP
HGSILNAWGK PVANYDDLKQ LGADLQKSSD FLLHAPVTPA KIGIFYDHEA DMGLRIEQYA
NDIRYYTDWT YRFYLALQDQ HLHRDVLMPG ADLKGYKLLY LPLLPMISDD HRAHLKTWVE
NGGTLILGPM TGYRTEYWTS FTDHAMVDIA EWSGIAVDSR IPVGTKLRPA EIPLKMTYNG
PLDLPEGQAG LWSEALSSKD GRVIAAYING MHAEKAAIME NTVGKGKVVL LGTDPGRGHL
GPLLRHYAKE QSIEPLVEGD AGPLVVHRKG IKQEGFILDN ITAEPKTIEL PKGKYTDILT
GKPYSAEQEL APYEVRVLQR K
//
