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Database: UniProt
Entry: A0A0N1BZY8_9PROT
LinkDB: A0A0N1BZY8_9PROT
Original site: A0A0N1BZY8_9PROT 
ID   A0A0N1BZY8_9PROT        Unreviewed;       800 AA.
AC   A0A0N1BZY8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=IP70_09560 {ECO:0000313|EMBL:KPF86604.1};
OS   alpha proteobacterium AAP38.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF86604.1, ECO:0000313|Proteomes:UP000037884};
RN   [1] {ECO:0000313|EMBL:KPF86604.1, ECO:0000313|Proteomes:UP000037884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP38 {ECO:0000313|EMBL:KPF86604.1,
RC   ECO:0000313|Proteomes:UP000037884};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:KPF86604.1}.
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DR   EMBL; LJHR01000009; KPF86604.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1BZY8; -.
DR   STRING; 1523418.IP70_09560; -.
DR   PATRIC; fig|1523418.3.peg.5206; -.
DR   Proteomes; UP000037884; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675}.
FT   DOMAIN          55..397
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
SQ   SEQUENCE   800 AA;  86569 MW;  FFE3BE2303AD3CE5 CRC64;
     MALAATFLSS GASLAETVLS VDATAPAPAL ETGYLKMGQG VSPAGGTIGI NNRYLTLDGK
     PWMPTMGEFH YTRFPADGWE EQLAKMKAAG IDIVATYIIW NHHEEVEGAF TWTGDRDLRR
     FAQLCAKHGL KLVVRIGPWS HAEVRYGGIP DWVVDAMPTR GNDPQYLSYV DRFYRQIAMQ
     VSGLLWKDGG PVIGVQLENE YNLTGPGQGR DHIATLKRMA LAAGFDVPLY TVTGWDQTVY
     PSGEVVPVFG GYPDEPWKAS PEILPPKETY AFRFDSRVSG NLGAQTVATR RGDADPDIPH
     TPFLGAEYGG GVPAMYRRRA VIDPADISAM LPVQIGSGVN LFGYYMFHGG RNPVGRTTLE
     ENTAIHGHND TPIIGYDFQA PIGQYGDMRP VLRKVRPFHL FTSAYGDQLA PMVPHAPAIL
     PKALDDLSTP RWSVRSAGDA AFLFFNSHIR QYRMQPVTDV RFTINLPGGP VSFPSEPVTI
     PAGSHFIWPV NMDLGGTRLA YATAQPVTRV TVDGIETHIL QAEPGVPVEL ALAGATDVRA
     PGAKVANRTR TTLVTGLKPG LGAVVTFKAA GAAKRLLILT EAQAESLALL RRNGHDIAVI
     SDADLFPTDA GFDLRSRGNP RFRYSTLPSL GRGGKTDGLF TTYEKAVTPK PDVPVTVEPV
     RAAQPAPAIR IGGPAKAAMQ PAPEAYGKSA AWSVRVPADA LAGVADAWLE LDYQGDVGRL
     FSGVRMIDDH YFNGPVWRIG LKRFAAEIAQ PLTLTVMPLR ADAPIYIQQE WKPAQKPDGQ
     VAVLKSARIV PEYALSVAVP
//
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