ID G1T115_RABIT Unreviewed; 654 AA.
AC G1T115;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000009723.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000009723.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000009723.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000009723.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_008246578.1; XM_008248356.1.
DR RefSeq; XP_008246579.1; XM_008248357.2.
DR AlphaFoldDB; G1T115; -.
DR SMR; G1T115; -.
DR STRING; 9986.ENSOCUP00000009723; -.
DR PaxDb; 9986-ENSOCUP00000009723; -.
DR Ensembl; ENSOCUT00000011297.3; ENSOCUP00000009723.3; ENSOCUG00000011296.3.
DR GeneID; 100345977; -.
DR KEGG; ocu:100345977; -.
DR eggNOG; KOG0496; Eukaryota.
DR GeneTree; ENSGT00950000182942; -.
DR HOGENOM; CLU_007853_7_2_1; -.
DR InParanoid; G1T115; -.
DR OrthoDB; 5489808at2759; -.
DR TreeFam; TF354299; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000011296; Expressed in testis and 5 other cell types or tissues.
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; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; BETA-GALACTOSIDASE RELATED; 1.
DR PANTHER; PTHR23421:SF59; BETA-GALACTOSIDASE-1-LIKE PROTEIN 3; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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:UP000001811}.
FT DOMAIN 80..390
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 450..549
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 573..632
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 227
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 301
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 654 AA; 74565 MW; 91D67844F149E228 CRC64;
MGSLRFLSRC LSWSRILAIF FLPFISSGLA PRSKLRETNP SQTAQPSEPR YNWSYVTPLE
LKNRSVGLGT GSTVTGHAHF TLNGHKFRIF GGSIHYFRVP REYWRDRLLK LKACGFNTVT
TYIPWNLHEP ETGKFDFSGN LDLKTFVTMA GEIGLWVILR AGPYICAEID LGGLPSRLLR
NPKAILRTTE KSFIEAVDRY FDHLVPRMAP LQFHQGGPVI AVQVENEYGS FNRDKRYMSY
LYQALVKRGI VELILTSDNE KEVLQGSTKG AFATVNLKEI KKDSFNQLHQ VQGNKPILIM
EFWVGWYSKW GDEQRFPKVY EVERTVSEFI KHELSFNAYM FHGGTNFGFM NGAAYTDEKH
WGVVTSYDYD AVLSEAGDYT EKYYRLRSLL GSASEIPLPQ LPDTNPKAVY PTVRLLHYLP
LWEVLEYLNE PVKSNSPINM ENLPINNGSG QSFGFTLYET PICSGGSLHA NAADTAQVFL
NETIVGFLDE HNQIMDIPKS TKCQHLRILV ENQGRINFSW KIQYENKGLI GPVSIDNVLL
KDFTIYPLEM KMNFFKRLRS ATWKPITGSY VGPAFYKGTL KAGSSPKDTF LSLMDWNKGF
VFINGHNLGR YWNIGPQKTL YLPGVWLHPG DNEIILFEKM ESGSSIQFKD KPQL
//
