ID A0A0N1ABX5_9PROT Unreviewed; 1000 AA.
AC A0A0N1ABX5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Probable beta-galactosidase B {ECO:0000256|ARBA:ARBA00040693};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase B {ECO:0000256|ARBA:ARBA00042633};
GN ORFNames=IP80_13880 {ECO:0000313|EMBL:KPF47661.1};
OS beta proteobacterium AAP65.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF47661.1, ECO:0000313|Proteomes:UP000037849};
RN [1] {ECO:0000313|EMBL:KPF47661.1, ECO:0000313|Proteomes:UP000037849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP65 {ECO:0000313|EMBL:KPF47661.1,
RC ECO:0000313|Proteomes:UP000037849};
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 -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000256|ARBA:ARBA00002691}.
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 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:KPF47661.1}.
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DR EMBL; LJHW01000026; KPF47661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1ABX5; -.
DR STRING; 1523424.IP80_13880; -.
DR PATRIC; fig|1523424.3.peg.1783; -.
DR Proteomes; UP000037849; 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; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF64; BETA-GALACTOSIDASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000037849};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 379..561
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1000 AA; 108850 MW; D8764B3CD5280CA3 CRC64;
MLAEDAARLD KATAPTGTPR QISWDQYSLK IDGQRQMIWA AEFQPFRLPS PSLWRDVLQK
YKAIGLNGVS LYFAWGYHSP HLGHYDFTGV RNLEKLLQIA KEEGLYVMVR PGPYVNAELS
MGGFPGWVTR QRGEARTDAP DYQAAAGEWL TQINAIIARY QLTTGGGTVI AYQLENEQFS
VQPKNARHMQ FLADKARADG ITVPLFHNAA SRLPDWTPKN STAPFANPGP TDLYAFDGYP
GGVCDVHGQP GNPVAAPDWG IYGKNFPRVG SLASPNTPGF GAEIGAGWFD YWGSNGTYNC
TAVRQGVGYQ RVFYGSNLIN RIVIHSIYMG FGGTTWGWQT APVVFTSYDY GAPITEARGL
RDKAYGLKAL GRFIQAAQPV LAQMDIGPVV APSNPRIKLY HNVNTALKSH VFFAVHNPSS
NTGTEAFSFD IDTADGRYRV PQAGTLQISG QDAKFMLAAV DLQRQRLAYS TSELWSHLRQ
GAHDLLVLHG RQGEDGETVL RYASRPRVKV LAGSVQQTWD AARGDLRLNY AHQGLIELEI
EGGGRAPLRL LIADDGAIAQ FWQLQAGADT VLVQSPALPR QARLEGATLA LQGDTESPSA
LRVWAAPEVK ALRWNGQPVA VATAAGASLA ARSPLAGPLQ AGRDYTLPDL AALPWQRRSD
SNEAEPGFDD SRWRAADAAG SAAQVWSASE RGAPVLAMSD YGFHRGDIWY RGRFKTTGTT
TTAGTPLELQ LYYGAGGAGL IQVWLNGKFI GQHELDAGRP FPETTDTFRL LLPALPTGEH
VLAVKVRNNG HNWDLFADDA HKEARGLIAA SLAPRAGRRH SLPISWKLRG APEAIGDLAR
GPYNNGGLGG EFLGWHLPSA PDRDLSTGWQ RVSPQAAPPA PGPYWLRTQF TLNLPEDHDV
QLGLAFGDTT VPRSPNAQYR VLIFVNGWHL GQFIAHIGPQ RVFVLPPGIV NPRGENTLAL
VVTSDGHSAN ALEDVKLVQL RSARGGVPLQ VLPPARYLQR
//
