GenomeNet

Database: UniProt
Entry: A0A1H8XUH2_9SPHI
LinkDB: A0A1H8XUH2_9SPHI
Original site: A0A1H8XUH2_9SPHI 
ID   A0A1H8XUH2_9SPHI        Unreviewed;       715 AA.
AC   A0A1H8XUH2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN05428947_11843 {ECO:0000313|EMBL:SEP43486.1};
OS   Mucilaginibacter sp. OK283.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1881049 {ECO:0000313|EMBL:SEP43486.1, ECO:0000313|Proteomes:UP000199509};
RN   [1] {ECO:0000313|EMBL:SEP43486.1, ECO:0000313|Proteomes:UP000199509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK283 {ECO:0000313|EMBL:SEP43486.1,
RC   ECO:0000313|Proteomes:UP000199509};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FODR01000018; SEP43486.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8XUH2; -.
DR   STRING; 1881049.SAMN05428947_11843; -.
DR   Proteomes; UP000199509; 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: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:SF2; BETA-GALACTOSIDASE YESZ; 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.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084}.
FT   DOMAIN          60..437
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          456..658
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          675..714
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        195
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   715 AA;  80860 MW;  1031063FFE930A33 CRC64;
     MKFMVKQLKT AAIEKPGTFL MRKLITTIIL GILIPSAALK AQEAGRFFPE KDLVTTGIYY
     YPEHWSEAQW ERDIKKISDM GFEFVHLAEF AWFKMEHEEG RFDFTWLDRV VGLCTKYHLK
     VLLCTPSATT PTWMRINYPE TFVMDGHYIR AENGTRGLES MVNPKFRGFV QRIVAEMAKR
     YGQNKNVMGW QVDNEPGAVP DYSPSSQDAF RTWLKNKYKT IDALNTAWGA AFWSQWFNSF
     DQVIIPNTNL VGWWGNNPHA LLDFKRYSAD AQAEFLDFQA GVLRSYVSKT QFVTTNYTAV
     CTGSDPNRTA KLDFATYTAY PNGGTDNLGE SGFRLGNSDV VLFASEYYKS VGGVSGVLEI
     QPGPVNWGSY NPLLLPGTVR LWLYHSFAAG GKVACSYRFR QILYGAEQYH AGVIQTDGVT
     PSQGGKDYMQ FMKEITELRK QFTPGAKMPA KLTARSTALL WNVENYWSID RQRQTGQWNT
     WDYPVKFLKT ARSLGAPVDV IQETADLSKY KCVIVPAYEM IDSALVKKWN DYVAKGGHLV
     ITCRTGTKDR RGHFWEGETA LPISNLIGAH ISQTDMLSSY GKGDILMNSN HYPWHSWADL
     LVPNDTAGVL ATYNNQFYKG KAAVVKHRIG KGDVTYIGVD TDDAKLEKDL LRQIYKDAGA
     TTEDYPPGVF VYWRDGFYTA LNYSSENYTV NLPDNAKVLI GEKTLKPSGV LVWTE
//
DBGET integrated database retrieval system