ID A0A0H3FDX5_RAHSY Unreviewed; 689 AA.
AC A0A0H3FDX5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 OrderedLocusNames=Rahaq_1590 {ECO:0000313|EMBL:ADW73212.1};
OS Rahnella sp. (strain Y9602).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Rahnella.
OX NCBI_TaxID=2703885 {ECO:0000313|EMBL:ADW73212.1, ECO:0000313|Proteomes:UP000007257};
RN [1] {ECO:0000313|Proteomes:UP000007257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y9602 {ECO:0000313|Proteomes:UP000007257};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Ovchinnikova G., Pagani I., Sobecky P.A., Martinez R.J.,
RA Woyke T.;
RT "Complete sequence of chromosome of Rahnella sp. Y9602.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW73212.1, ECO:0000313|Proteomes:UP000007257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y9602 {ECO:0000313|EMBL:ADW73212.1,
RC ECO:0000313|Proteomes:UP000007257};
RX PubMed=22461551; DOI=10.1128/JB.00095-12;
RA Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA Tapia R., Woyke T., Sobecky P.A.;
RT "Complete Genome Sequence of Rahnella sp. Strain Y9602, a
RT Gammaproteobacterium Isolate from Metal- and Radionuclide-Contaminated
RT Soil.";
RL J. Bacteriol. 194:2113-2114(2012).
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; CP002505; ADW73212.1; -; Genomic_DNA.
DR RefSeq; WP_013574914.1; NC_015061.1.
DR AlphaFoldDB; A0A0H3FDX5; -.
DR KEGG; rah:Rahaq_1590; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_012430_1_1_6; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000007257; 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: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 InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR Pfam; PF02449; Glyco_hydro_42; 1.
DR Pfam; PF08533; Glyco_hydro_42C; 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, ECO:0000313|EMBL:ADW73212.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ADW73212.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 19..391
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 403..615
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 626..682
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 314
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 689 AA; 77257 MW; A4E8540A21454265 CRC64;
MTKFPLLSSK ISGLLHGADY NPEQWLESPD VLIRDVEMMK EARCNVMSVG IFSWSALEPE
EGHFTFGWLD QVLDKLHENG ISVFLATPSG ARPAWMSQKY PEVLRVGRDR VKALHGGRHN
HCMSSPVYAE KVQLMNSALA KRYAHHPAVI GWHISNEYGG ECHCHYCQTR FRDWLKARYV
TLDALNQAWW STFWSHTYTD WAQIESPSPQ GESGIHGLNL DWRRFNTDQV TRFCSEEIRP
LKAENPALPA TTNFMEYFYD YDYWKLASVL DFISWDSYPM WHTRNDDIGL AAYTAMYHDL
MRTLKQGQPF VLMESTPSFT NWQPVSKLKK PGMHILSSLQ AVAHGSDSVQ YFQWRKSRGS
SEKFHGAVVD HVGHIDTRVG REVAELGGIL SALAPVAGSR VEARVAIIFD WESRWAMDDS
LGPRNQGLEY ENTVAGHYRA LWSQGIAVDV INADCDLTGY DLVIAPMLYM VRAGVGERIT
AFVQAGGRFV ATYWSGIVNE SDLCFLNGFP GPLRPVLGIW AEEIDSLTDD QHNSVSGTEG
NALGLNGPYR ASELCEVIHL EGAAALATYG DDFYAGTPAV TVNLFGKGQA YYLASRNDQQ
FHADFYTALA KEMKLPRAIA TDLPEGVTAA RRTDGESEFI FLQNYAADSQ TVTLPDDYRD
MVHGGILPRT LTLPAFGCQI LSRRLSVIS
//