ID   BGAL4_ARATH             Reviewed;         724 AA.
AC   Q9SCV8; Q56WL4; Q93Y27;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Beta-galactosidase 4;
DE            Short=Lactase 4;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
GN   Name=BGAL4; OrderedLocusNames=At5g56870; ORFNames=MPI10.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 526-724.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=16267099; DOI=10.1093/pcp/pci223;
RA   Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.;
RT   "Apoplastic glycosidases active against xyloglucan oligosaccharides of
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 47:55-63(2006).
RN   [7]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, GENE FAMILY,
RP   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).
RN   [8]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17234672; DOI=10.1093/pcp/pcm009;
RA   Lee E.-J., Matsumura Y., Soga K., Hoson T., Koizumi N.;
RT   "Glycosyl hydrolases of cell wall are induced by sugar starvation in
RT   Arabidopsis.";
RL   Plant Cell Physiol. 48:405-413(2007).
CC   -!- FUNCTION: Preferentially hydrolyzes para-nitrophenyl-beta-D-
CC       galactoside. Can hydrolyze para-nitrophenyl-beta-D-fucoside with 5 time
CC       less efficiency. {ECO:0000269|PubMed:17466346}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.4 uM for para-nitrophenyl-beta-D-galactoside
CC         {ECO:0000269|PubMed:17466346};
CC         KM=2.2 uM for ortho-nitrophenyl-beta-D-galactoside
CC         {ECO:0000269|PubMed:17466346};
CC         Vmax=467 nmol/sec/mg enzyme with para-nitrophenyl-beta-D-galactoside
CC         as substrate {ECO:0000269|PubMed:17466346};
CC         Vmax=1630 nmol/sec/mg enzyme with
CC         ortho-nitrophenyl-beta-D-galactoside as substrate
CC         {ECO:0000269|PubMed:17466346};
CC         Note=Measured at pH 4.5 and 37 degrees Celsius for all experiments.;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305|PubMed:17234672}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with higher expression levels in roots
CC       and siliques. {ECO:0000269|PubMed:16267099,
CC       ECO:0000269|PubMed:17234672, ECO:0000269|PubMed:17466346}.
CC   -!- INDUCTION: By sugar starvation and exposure to darkness for 24 hours.
CC       {ECO:0000269|PubMed:17234672}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ270300; CAB64740.1; -; mRNA.
DR   EMBL; AB020747; BAA97206.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96817.1; -; Genomic_DNA.
DR   EMBL; AY054589; AAK96780.1; -; mRNA.
DR   EMBL; AY064690; AAL47393.1; -; mRNA.
DR   EMBL; AK222026; BAD94714.1; -; mRNA.
DR   RefSeq; NP_200498.1; NM_125070.3.
DR   AlphaFoldDB; Q9SCV8; -.
DR   SMR; Q9SCV8; -.
DR   BioGRID; 21033; 1.
DR   STRING; 3702.Q9SCV8; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q9SCV8; 1 site, No reported glycans.
DR   PaxDb; 3702-AT5G56870-1; -.
DR   ProteomicsDB; 240419; -.
DR   EnsemblPlants; AT5G56870.1; AT5G56870.1; AT5G56870.
DR   GeneID; 835789; -.
DR   Gramene; AT5G56870.1; AT5G56870.1; AT5G56870.
DR   KEGG; ath:AT5G56870; -.
DR   Araport; AT5G56870; -.
DR   TAIR; AT5G56870; BGAL4.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; Q9SCV8; -.
DR   OMA; THFEQWN; -.
DR   OrthoDB; 5489808at2759; -.
DR   PhylomeDB; Q9SCV8; -.
DR   BioCyc; ARA:AT5G56870-MONOMER; -.
DR   SABIO-RK; Q9SCV8; -.
DR   PRO; PR:Q9SCV8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9SCV8; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004565; F:beta-galactosidase activity; TAS:TAIR.
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; IPR048913; BetaGal_gal-bd.
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:SF146; BETA-GALACTOSIDASE 4; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 2.
DR   Pfam; PF17834; GHD; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   Genevisible; Q9SCV8; AT.
PE   1: Evidence at protein level;
KW   Apoplast; Glycoprotein; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..724
FT                   /note="Beta-galactosidase 4"
FT                   /id="PRO_5000065879"
FT   ACT_SITE        185
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        254
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        255
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        290
FT                   /note="V -> I (in Ref. 4; AAK96780/AAL47393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        561
FT                   /note="V -> A (in Ref. 5; BAD94714)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   724 AA;  80591 MW;  57D314FEA3C9861D CRC64;
     MVLNFRDKSC IFLAILCCLS LSCIVKASVS YDRKAVIING QRRILLSGSI HYPRSTPEMW
     PGLIQKAKEG GLDVIETYVF WNGHEPSPGQ YYFGDRYDLV KFIKLVHQAG LYVNLRIGPY
     VCAEWNFGGF PVWLKFVPGM AFRTDNEPFK AAMKKFTEKI VWMMKAEKLF QTQGGPIILA
     QIENEYGPVE WEIGAPGKAY TKWVAQMALG LSTGVPWIMC KQEDAPGPII DTCNGYYCED
     FKPNSINKPK MWTENWTGWY TDFGGAVPYR PVEDIAYSVA RFIQKGGSLV NYYMYHGGTN
     FDRTAGEFMA SSYDYDAPLD EYGLPREPKY SHLKALHKAI KLSEPALLSA DATVTSLGAK
     QEAYVFWSKS SCAAFLSNKD ENSAARVLFR GFPYDLPPWS VSILPDCKTE VYNTAKVNAP
     SVHRNMVPTG TKFSWGSFNE ATPTANEAGT FARNGLVEQI SMTWDKSDYF WYITDITIGS
     GETFLKTGDS PLLTVMSAGH ALHVFVNGQL SGTAYGGLDH PKLTFSQKIK LHAGVNKIAL
     LSVAVGLPNV GTHFEQWNKG VLGPVTLKGV NSGTWDMSKW KWSYKIGVKG EALSLHTNTE
     SSGVRWTQGS FVAKKQPLTW YKSTFATPAG NEPLALDMNT MGKGQVWING RNIGRHWPAY
     KAQGSCGRCN YAGTFDAKKC LSNCGEASQR WYHVPRSWLK SQNLIVVFEE LGGDPNGISL
     VKRT
//