BGAL4_ARATH
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 03-AUG-2022, entry version 132.
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 ortho-nitrophenyl-beta-D-
CC galactoside as substrate {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}.
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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.AT5G56870.1; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR PaxDb; Q9SCV8; -.
DR PRIDE; Q9SCV8; -.
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; locus:2170282; AT5G56870.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR InParanoid; Q9SCV8; -.
DR OMA; MNSAVKV; -.
DR OrthoDB; 179316at2759; -.
DR PhylomeDB; Q9SCV8; -.
DR BioCyc; ARA:AT5G56870-MON; -.
DR SABIO-RK; Q9SCV8; -.
DR PRO; PR:Q9SCV8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SCV8; baseline and differential.
DR Genevisible; Q9SCV8; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; HDA: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 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
