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Database: UniProt
Entry: A0A1Y4DEI2_9BACT
LinkDB: A0A1Y4DEI2_9BACT
Original site: A0A1Y4DEI2_9BACT 
ID   A0A1Y4DEI2_9BACT        Unreviewed;       895 AA.
AC   A0A1Y4DEI2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=B5F77_04585 {ECO:0000313|EMBL:OUO53881.1};
OS   Parabacteroides sp. An277.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=1965619 {ECO:0000313|EMBL:OUO53881.1, ECO:0000313|Proteomes:UP000196154};
RN   [1] {ECO:0000313|Proteomes:UP000196154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An277 {ECO:0000313|Proteomes:UP000196154};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:OUO53881.1}.
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DR   EMBL; NFJB01000008; OUO53881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4DEI2; -.
DR   OrthoDB; 703126at2; -.
DR   Proteomes; UP000196154; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196154};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..895
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013232121"
FT   DOMAIN          59..392
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
SQ   SEQUENCE   895 AA;  103249 MW;  18F742103D41A493 CRC64;
     MNVKTFCCML LLVAGNISAQ YKIDLSSIEC PKIEYLKLGN PGPKGREIRI NNLYWEEAGK
     PKLPVMGEFH YNRMDERYWK EALMKMKASG VNIVSTYTLW ILHEEFEGRQ DWSGRNNLRK
     FVELCQEVGL QVHLRLGPYC NAEIRNGGFP DWIEFNKKLK PRTNDPLYLN YVRYWYQSLF
     NQIKGLLYKD GGPIVAIQLE NEYVTEGMVI PHLMALKKIA IEVGFDVPVY SMTHWMMSDY
     PKGEIIPYAG YYLETPWISF GNKENPTTDQ EFFTYNRISD NIGNDFIKTN AKVETLDDET
     NDSPYFTCEM GLGSPNYYMR RAVVPEEMAG ENINLRLGCG VNLMGYYMYV GQTNPIAEQY
     TTARATARIS NDYQAPIREF GQMGVALKEA KKLNYFMNDF GSQLVLKRAF LPITNQNREN
     LQWAVRTDGK SGYVFCSNIL HKHPRKEYHH VQFELDLNEE KICLPHKKVT IQDRSYFFWP
     FNLDLQGIIL KYATAQPICY LDENDTRYYF FFEDDGIPAE FCFKTENVQD VQALNGKVKR
     LKDVYFVDEL QAGKDCQIKV KAKNGSSICI TLLTEKESDY IWKGEVNGKK FVSLSESFIY
     FDKNDIFIAS ENPSQTIDLF TKGKFTTQTY SSEYISRKAK AVIVPPMEKA LCIRPLKGNI
     VKRIFDARSM STIEHAYLRM QATEETKVFI NGKEIATSNY QGYRYADVSK ACRIGMNEIC
     FQTGNTQEGI TAEIEVLLAN GTRWLWNTDE LWYDTDGHTP VKTEIPIHKL TKYDDREHLA
     VFQVALPTNM CPDIATRLYI NATGDVANAY LGQHLIHDVF INGADWIIGL NRYTKLIEEN
     PLLTIRINGL KSIDSGIYFE KNISRTDCLQ PVIRNIHMEQ EYVLPLKLST KAPKP
//
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