BGAL5_ARATH
ID BGAL5_ARATH Reviewed; 732 AA.
AC Q9MAJ7; Q93Z63; Q9SCV7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Beta-galactosidase 5;
DE Short=Lactase 5;
DE EC=3.2.1.23;
DE Flags: Precursor;
GN Name=BGAL5; OrderedLocusNames=At1g45130; ORFNames=F27F5.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gy I., Kreis M., Lecharny A.;
RT "The beta-galactosidases are encoding by a multigene family in Arabidopsis
RT thaliana.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17466346; DOI=10.1016/j.phytochem.2007.03.021;
RA Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P.,
RA Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 35.";
RL Phytochemistry 68:1510-1520(2007).
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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC {ECO:0000269|PubMed:17466346}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AJ270301; CAB64741.1; -; mRNA.
DR EMBL; AC007915; AAF69162.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32082.1; -; Genomic_DNA.
DR EMBL; AY058098; AAL24206.1; -; mRNA.
DR EMBL; AY069911; AAL47461.1; -; mRNA.
DR EMBL; AY093977; AAM16238.1; -; mRNA.
DR RefSeq; NP_175127.1; NM_103587.3.
DR AlphaFoldDB; Q9MAJ7; -.
DR SMR; Q9MAJ7; -.
DR STRING; 3702.AT1G45130.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR iPTMnet; Q9MAJ7; -.
DR PaxDb; Q9MAJ7; -.
DR PRIDE; Q9MAJ7; -.
DR ProteomicsDB; 240760; -.
DR EnsemblPlants; AT1G45130.1; AT1G45130.1; AT1G45130.
DR GeneID; 841080; -.
DR Gramene; AT1G45130.1; AT1G45130.1; AT1G45130.
DR KEGG; ath:AT1G45130; -.
DR Araport; AT1G45130; -.
DR TAIR; locus:2028265; AT1G45130.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9MAJ7; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q9MAJ7; -.
DR BioCyc; ARA:AT1G45130-MON; -.
DR BRENDA; 3.2.1.23; 399.
DR PRO; PR:Q9MAJ7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAJ7; baseline and differential.
DR Genevisible; Q9MAJ7; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041392; GHD.
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; PTHR23421; 1.
DR Pfam; PF17834; GHD; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..732
FT /note="Beta-galactosidase 5"
FT /id="PRO_5000065880"
FT ACT_SITE 187
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 453
FT /note="R -> P (in Ref. 1; CAB64741)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="V -> A (in Ref. 1; CAB64741)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="A -> V (in Ref. 4; AAL24206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 81444 MW; 0442C83D04F7CBC4 CRC64;
MGTTILVLSK ILTFLLTTML IGSSVIQCSS VTYDKKAIVI NGHRRILLSG SIHYPRSTPE
MWEDLIKKAK DGGLDVIDTY VFWNGHEPSP GTYNFEGRYD LVRFIKTIQE VGLYVHLRIG
PYVCAEWNFG GFPVWLKYVD GISFRTDNGP FKSAMQGFTE KIVQMMKEHR FFASQGGPII
LSQIENEFEP DLKGLGPAGH SYVNWAAKMA VGLNTGVPWV MCKEDDAPDP IINTCNGFYC
DYFTPNKPYK PTMWTEAWSG WFTEFGGTVP KRPVEDLAFG VARFIQKGGS YINYYMYHGG
TNFGRTAGGP FITTSYDYDA PIDEYGLVQE PKYSHLKQLH QAIKQCEAAL VSSDPHVTKL
GNYEEAHVFT AGKGSCVAFL TNYHMNAPAK VVFNNRHYTL PAWSISILPD CRNVVFNTAT
VAAKTSHVQM VPSGSILYSV ARYDEDIATY GNRGTITARG LLEQVNVTRD TTDYLWYTTS
VDIKASESFL RGGKWPTLTV DSAGHAVHVF VNGHFYGSAF GTRENRKFSF SSQVNLRGGA
NKIALLSVAV GLPNVGPHFE TWATGIVGSV VLHGLDEGNK DLSWQKWTYQ AGLRGESMNL
VSPTEDSSVD WIKGSLAKQN KQPLTWYKAY FDAPRGNEPL ALDLKSMGKG QAWINGQSIG
RYWMAFAKGD CGSCNYAGTY RQNKCQSGCG EPTQRWYHVP RSWLKPKGNL LVLFEELGGD
ISKVSVVKRS VN
