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
//