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Q9SCV8 (BGAL4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-galactosidase 4

Short name=Lactase 4
EC=3.2.1.23
Gene names
Name:BGAL4
Ordered Locus Names:At5g56870
ORF Names:MPI10.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length724 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Preferentially hydrolyzes para-nitrophenyl-beta-D-galactoside. Can hydrolyze para-nitrophenyl-beta-D-fucoside with 5 time less efficiency. Ref.7

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.

Subcellular location

Secretedextracellular spaceapoplast Probable Ref.8.

Tissue specificity

Ubiquitous, with higher expression levels in roots and siliques. Ref.6 Ref.7 Ref.8

Induction

By sugar starvation and exposure to darkness for 24 hours. Ref.8

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Biophysicochemical properties

Kinetic parameters:

Measured at pH 4.5 and 37 degrees Celsius for all experiments.

KM=3.4 µM for para-nitrophenyl-beta-D-galactoside Ref.7

KM=2.2 µM for ortho-nitrophenyl-beta-D-galactoside

Vmax=467 nmol/sec/mg enzyme with para-nitrophenyl-beta-D-galactoside as substrate

Vmax=1630 nmol/sec/mg enzyme with ortho-nitrophenyl-beta-D-galactoside as substrate

Ontologies

Keywords
   Cellular componentApoplast
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-galactosidase activity

Traceable author statement PubMed 15517348. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 724697Beta-galactosidase 4
PRO_5000065879

Sites

Active site1851Proton donor Potential
Active site2541Nucleophile Potential

Amino acid modifications

Glycosylation2551N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2901V → I in AAK96780. Ref.4
Sequence conflict2901V → I in AAL47393. Ref.4
Sequence conflict5611V → A in BAD94714. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9SCV8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 57D314FEA3C9861D

FASTA72480,591
        10         20         30         40         50         60 
MVLNFRDKSC IFLAILCCLS LSCIVKASVS YDRKAVIING QRRILLSGSI HYPRSTPEMW 

        70         80         90        100        110        120 
PGLIQKAKEG GLDVIETYVF WNGHEPSPGQ YYFGDRYDLV KFIKLVHQAG LYVNLRIGPY 

       130        140        150        160        170        180 
VCAEWNFGGF PVWLKFVPGM AFRTDNEPFK AAMKKFTEKI VWMMKAEKLF QTQGGPIILA 

       190        200        210        220        230        240 
QIENEYGPVE WEIGAPGKAY TKWVAQMALG LSTGVPWIMC KQEDAPGPII DTCNGYYCED 

       250        260        270        280        290        300 
FKPNSINKPK MWTENWTGWY TDFGGAVPYR PVEDIAYSVA RFIQKGGSLV NYYMYHGGTN 

       310        320        330        340        350        360 
FDRTAGEFMA SSYDYDAPLD EYGLPREPKY SHLKALHKAI KLSEPALLSA DATVTSLGAK 

       370        380        390        400        410        420 
QEAYVFWSKS SCAAFLSNKD ENSAARVLFR GFPYDLPPWS VSILPDCKTE VYNTAKVNAP 

       430        440        450        460        470        480 
SVHRNMVPTG TKFSWGSFNE ATPTANEAGT FARNGLVEQI SMTWDKSDYF WYITDITIGS 

       490        500        510        520        530        540 
GETFLKTGDS PLLTVMSAGH ALHVFVNGQL SGTAYGGLDH PKLTFSQKIK LHAGVNKIAL 

       550        560        570        580        590        600 
LSVAVGLPNV GTHFEQWNKG VLGPVTLKGV NSGTWDMSKW KWSYKIGVKG EALSLHTNTE 

       610        620        630        640        650        660 
SSGVRWTQGS FVAKKQPLTW YKSTFATPAG NEPLALDMNT MGKGQVWING RNIGRHWPAY 

       670        680        690        700        710        720 
KAQGSCGRCN YAGTFDAKKC LSNCGEASQR WYHVPRSWLK SQNLIVVFEE LGGDPNGISL 


VKRT 

« Hide

References

« Hide 'large scale' references
[1]"The beta-galactosidases are encoding by a multigene family in Arabidopsis thaliana."
Gy I., Kreis M., Lecharny A.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 526-724.
Strain: cv. Columbia.
[6]"Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana."
Iglesias N., Abelenda J.A., Rodino M., Sampedro J., Revilla G., Zarra I.
Plant Cell Physiol. 47:55-63(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 35."
Ahn Y.O., Zheng M., Bevan D.R., Esen A., Shiu S.-H., Benson J., Peng H.-P., Miller J.T., Cheng C.-L., Poulton J.E., Shih M.-C.
Phytochemistry 68:1510-1520(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
[8]"Glycosyl hydrolases of cell wall are induced by sugar starvation in Arabidopsis."
Lee E.-J., Matsumura Y., Soga K., Hoson T., Koizumi N.
Plant Cell Physiol. 48:405-413(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ270300 mRNA. Translation: CAB64740.1.
AB020747 Genomic DNA. Translation: BAA97206.1.
CP002688 Genomic DNA. Translation: AED96817.1.
AY054589 mRNA. Translation: AAK96780.1.
AY064690 mRNA. Translation: AAL47393.1.
AK222026 mRNA. Translation: BAD94714.1.
RefSeqNP_200498.1. NM_125070.2.
UniGeneAt.21539.

3D structure databases

ProteinModelPortalQ9SCV8.
SMRQ9SCV8. Positions 28-724.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid21033. 1 interaction.
STRING3702.AT5G56870.1-P.

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.

Proteomic databases

PaxDbQ9SCV8.
PRIDEQ9SCV8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G56870.1; AT5G56870.1; AT5G56870.
GeneID835789.
KEGGath:AT5G56870.

Organism-specific databases

GeneFarm493. 90.
TAIRAT5G56870.

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000239919.
InParanoidQ9SCV8.
OMAWSKSSCA.
PhylomeDBQ9SCV8.

Enzyme and pathway databases

BioCycARA:AT5G56870-MONOMER.
SABIO-RKQ9SCV8.

Gene expression databases

GenevestigatorQ9SCV8.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
3.20.20.80. 1 hit.
InterProIPR008979. Galactose-bd-like.
IPR019801. Glyco_hydro_35_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR001944. Glycoside_Hdrlase_35.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR23421. PTHR23421. 1 hit.
PfamPF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSPR00742. GLHYDRLASE35.
SUPFAMSSF49785. SSF49785. 3 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGAL4_ARATH
AccessionPrimary (citable) accession number: Q9SCV8
Secondary accession number(s): Q56WL4, Q93Y27
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names