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Database: UniProt
Entry: A0A255Y018_9PROT
LinkDB: A0A255Y018_9PROT
Original site: A0A255Y018_9PROT 
ID   A0A255Y018_9PROT        Unreviewed;       664 AA.
AC   A0A255Y018;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=CHR90_00865 {ECO:0000313|EMBL:OYQ21965.1};
OS   Elstera cyanobacteriorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Elstera.
OX   NCBI_TaxID=2022747 {ECO:0000313|EMBL:OYQ21965.1, ECO:0000313|Proteomes:UP000216361};
RN   [1] {ECO:0000313|EMBL:OYQ21965.1, ECO:0000313|Proteomes:UP000216361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH019 {ECO:0000313|EMBL:OYQ21965.1,
RC   ECO:0000313|Proteomes:UP000216361};
RA   Cai H.;
RT   "Elstera cyanobacteriorum sp. nov., a novel bacterium isolated from
RT   cyanobacterial aggregates in a eutrophic lake.";
RL   Submitted (JUL-2017) 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:OYQ21965.1}.
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DR   EMBL; NOXS01000018; OYQ21965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255Y018; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000216361; 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: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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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; IPR013780; Glyco_hydro_b.
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.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216361}.
FT   DOMAIN          5..387
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          399..594
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   ACT_SITE        141
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        313
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   664 AA;  75133 MW;  F0626C238F9B9E60 CRC64;
     MLGVCYYPEH WNESQWADDA RRMVELGIRI VRIGEFAWTR LEPNPGEYRF EWLDRAIETL
     GGAGLKIVLG TPTTTPPKWL IDQMPDMIAY DRDGRPRGFG SRRHYDFSHE GYRREVARIT
     EVLAKRYGKN PHIMAWQLDN EYGCHDTIRS YSPVARRAFQ EWLRARYRTI AALNQAWGTV
     FWSMELRDFN EAELPNLTVT EANPSAWLDF YRFASDQVVS FNKLKADILR HHAPGQDLSH
     NYMGFITEFD HFKVAADLDF ATWDSYPLGF TDTLLRLPPE ERQRWQRTGH PDIAAFHHDL
     YRAVGRGRWW VMEQQPGPVN WAFHNPAPLP GMVRLWTWEA FAHGAEVVTY FRWRQVPFAQ
     EQMHAGLLRP DSEPAPGYAE AGAVAVEAAD LPMPDTEPAP VAILFDYAAD WLLTAHPQGR
     EYSFKHIVFD WYQAVRRLGL DVDFVSPDGD PSAYRLILAP ASPLVSDALA ARLAQAVASG
     ATLVLGPRVG SKTENLHIPS NLAPGALATL AGFRVERVES LDPAFAEPVT WHGETYQTRG
     WREATEGGAK VLATFNDGWP ALREQRHGAG RVYSWHGLPD GDFLRAVLAP WAEAVGLTLH
     PVPETVRLRR RGSLTFAFNY GSDPWHGPVE GASGVRYRIG GARVLPQQIA AWERSPSHDP
     MGVE
//
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