ID B9RGA7_RICCO Unreviewed; 1110 AA.
AC B9RGA7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=RCOM_1452500 {ECO:0000313|EMBL:EEF49562.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; EQ973778; EEF49562.1; -; Genomic_DNA.
DR RefSeq; XP_002513059.1; XM_002513013.2.
DR AlphaFoldDB; B9RGA7; -.
DR STRING; 3988.B9RGA7; -.
DR GeneID; 8270882; -.
DR KEGG; rcu:8270882; -.
DR eggNOG; KOG2024; Eukaryota.
DR InParanoid; B9RGA7; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005990; P:lactose catabolic process; IBA:GO_Central.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311}.
FT DOMAIN 809..1092
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1110 AA; 125702 MW; 41E8953F063F0DB9 CRC64;
MASLAANMVS PLETGHKVWE DPSFIKWRKR EPHVTLHCHE SVEGSLRYWY QRNKVDVLVS
KSAVWNDDAV KAALDCAAFW VKDLPFVKSM SGFWKFFLAP SPTKVPIKFY EPAFQDFEWQ
TLPVPSNWQM HGFDRPIYTN VVYPFPLDPP YVPEDNPTGC YRTYFQIPKE WQGRRILLHF
EAVDSAFCAW VNGVPVGYSQ DSRLPAEFEI TEYCYSCDSG KSNVLAVQVI RWSDGSYLED
QDHWWLSGIH RDVLLLAKPQ VFIVDYFFKS NLAEDFASAE IEVEVKLDSS QEMPKDKILD
NFVIEAALYD TESWYNSDGA ANLLSSQVAD IKINPSFDAI LGFLGYVLVG KVEKPKLWSA
EQPNLYILVL TLKDAFGHVV DCESCLVGIR QVSKAPKQLL VNGQPVIIRG VNRHEHHPRI
GKTNIESCMI KDLVLMKQNN INAVRNSHYP QHPRWYELCD LFGMYMIDEA NIETHGFHLS
GHIKHPTSEQ SWAIAMIDRV IGMVERDKNH ACIISWSLGN EASYGPNHSA AAGWIRGKDT
SRLVHYEGGG SRTPSTDIVC PMYMRVWDIV KIANDPTELR PLILCEYSHA MGNSSGNICE
YWEAIDSTFG LQGGFIWDWV DQGLLKENTD GSKYWAYGGD FGDTPNDLNF CLNGLTWPDR
SPHPALHEVK YVYQPIKVSL KGSTLKITNT YFFETTQGLE FSWAAHGDGH QLGSGILSLP
LMKPQSSYDI ELESGPWYPL WASYSGEIFL TVTAKLLHST PWVETGHVIS STQVQLPSRK
EIIPHVIKAT DATLSSEILG DTVRVSQQTF WEITLNIQTG TVESWKVEGV TIMNKGILPC
FWRAPTDNDK GGEENSYYSR WKAARIDNLE FLTKSCSIQE KTDHLVKIKA VYIGVPRDED
DSSQSSKQAL FEVDIIYEIF GSGDLIIECN VSPSSDLPPL PRVGVEFHLV ESVDHVRWYG
KGPFECYPDR KAASHVGIYE KNVCDMHVPY IVPGECSGRA DVRWVTFQNK EGKGIFASMH
GNSPPMQMSV SYYSTRELHR ARHNKELVRG NDIEVHLDHK HMGIGGDDSW SPCVHEKYLV
PAVPYSFSIR LCPITAATSG LRIYEPEHQN
//