ID A0A0M4LPV9_9GAMM Unreviewed; 635 AA.
AC A0A0M4LPV9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=W908_05200 {ECO:0000313|EMBL:ALE01997.1};
OS Candidatus Pseudothioglobus singularis PS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01997.1, ECO:0000313|Proteomes:UP000068905};
RN [1] {ECO:0000313|EMBL:ALE01997.1, ECO:0000313|Proteomes:UP000068905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS1 {ECO:0000313|EMBL:ALE01997.1,
RC ECO:0000313|Proteomes:UP000068905};
RX PubMed=26494659;
RA Marshall K.T., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01155-e01115(2015).
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}.
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DR EMBL; CP006911; ALE01997.1; -; Genomic_DNA.
DR RefSeq; WP_053820213.1; NZ_CP006911.1.
DR AlphaFoldDB; A0A0M4LPV9; -.
DR STRING; 1125411.W908_05200; -.
DR KEGG; tsn:W908_05200; -.
DR PATRIC; fig|1125411.7.peg.1024; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000068905; 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:0005975; P:carbohydrate 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 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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR Pfam; PF02449; Glyco_hydro_42; 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};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000068905};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 8..392
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 402..588
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 635 AA; 72797 MW; B0652BCB61131E8F CRC64;
MKPKLGSCYY PEHWPEERWQ KDAEEMVAAG LSWVRIGEFA WSRLEPEQGV QNFDWLDRAI
SILGNVGLNI VMSTPTAAPP RWVVDKCPDM LLVDVEGRSR QFGSRRHYCF SHEGYLEESL
RISKAVAERY GNNPFIKAWQ LDNEYGCHDT TLSYSPSALK AFRNWIAKKY ESIDQLNKAW
KNVFWSMEYN SFDQVGLPNL TVTDPNPIHE LDFKRFSSDQ VVNFNRSQAS VMRQYTKMPL
IHNYMGRITD FNHYDVGKDL DIASWDSYPL GFLEDRSTQD DEFKLRFMRH GDPDFQAFHH
DLYRTVGQGR WWVMEQQPGP VNWAPYNPEP APGAVRLWSW EAIAHGAEVV SYFRWRQAPF
AQEQMHAGLQ RPDGENAPGI TQASQVSSEL KEFKDIEQVQ SKIALIFDYE SCWAWEIQPQ
GKGFDYFELV YDNYRALRSL GLSVDILPPN QSDLKGYKVV LMPGLMRVSR ELEDAIESFE
GVLISGPRAG SKTTNMSIPS QLPPIVPGVK ATVASAETLR PNAFISIKGL GSFKTWMETL
IDYDNIIEET EDGRAAVVGH EKNIYIAGWA DQMTLKMIFS RVCESKDIST TKLEDCVRVR
ETLTHRFWFN YSNQECNVGS VCIPPSGVIW ESIKG
//
