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Database: UniProt/TrEMBL
Entry: A0A0H3FDX5_RAHSY
LinkDB: A0A0H3FDX5_RAHSY
Original site: A0A0H3FDX5_RAHSY 
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
//
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