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Q7G3T8 (BGA13_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 58. 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 13

Short name=Lactase 13
EC=3.2.1.23
Gene names
Ordered Locus Names:Os10g0330600, LOC_Os10g18400
ORF Names:OsJ_029894, OSJNAb0008A05.15, OSJNBb0008A05.25
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length828 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Secretedextracellular spaceapoplast Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 35 family.

Contains 1 SUEL-type lectin domain.

Sequence caution

The sequence AAL31090.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAN04162.1 differs from that shown. Reason: Erroneous initiation.

The sequence EAZ15685.1 differs from that shown. Reason: Erroneous initiation.

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

Inferred from electronic annotation. Source: UniProtKB-EC

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 828805Beta-galactosidase 13
PRO_0000294165

Regions

Domain746 – 82883SUEL-type lectin

Sites

Active site1871Proton donor Potential
Active site2591Nucleophile Potential

Amino acid modifications

Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation5021N-linked (GlcNAc...) Potential
Glycosylation5781N-linked (GlcNAc...) Potential
Glycosylation5861N-linked (GlcNAc...) Potential
Glycosylation6151N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict4201S → N in AK119350. Ref.5
Sequence conflict5211H → R in AK119350. Ref.5
Sequence conflict8171C → G in EAZ15685. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q7G3T8 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: C0DE893C51D7D2B8

FASTA82892,000
        10         20         30         40         50         60 
MKTTMAAAAT CLVALLVVVL AEAAGVGCTT VAYNDRSLVI DGERRIIISG SIHYPRSTPE 

        70         80         90        100        110        120 
MWPDLIKKAK EGGLDAIETY VFWNGHEPHR RQYNFEGNYD IIRFFKEIQN AGLYAILRIG 

       130        140        150        160        170        180 
PYICGEWNYG GLPAWLRDIP QMQFRMHNAP FENEMENFTT LIINKMKDAN MFAGQGGPII 

       190        200        210        220        230        240 
LAQIENEYGN VMGQLNNNQS ASEYIHWCAD MANKQNVGVP WIMCQQDSDV PHNVVNTCNG 

       250        260        270        280        290        300 
FYCHDWFPNR TGIPKIWTEN WTGWFKAWDK PDFHRSAEDI AFAVAMFFQK RGSLQNYYMY 

       310        320        330        340        350        360 
HGGTNFGRTS GGPYITTSYD YDAPLDEYGN LRQPKYGHLK DLHSVIKSIE KILVHGEYVD 

       370        380        390        400        410        420 
ANYSDNVTVT KYTLGSTSAC FINNRNDNKD LNVTLDGNTH LLPAWSVSIL PDCKTVAFNS 

       430        440        450        460        470        480 
AKIKAQTTIM VKKANMVEKE PESLKWSWMR ENLTPFMTDE KGSYRKNELL EQIVTSTDQS 

       490        500        510        520        530        540 
DYLWYRTSLD HKGEASYTLF VNTTGHELYA FVNGMLVGKN HSPNGHFVFQ LESAVKLHDG 

       550        560        570        580        590        600 
KNYISLLSAT IGLKNYGPLF EKMPAGIVGG PVKLIDNNGT GIDLSNSSWS YKAGLAGEYR 

       610        620        630        640        650        660 
QIHLDKPGYR WDNNNGTVPI NRPFTWYKTT FQAPAGQDTV VVDLLGLNKG VAWVNGNNLG 

       670        680        690        700        710        720 
RYWPSYTAAE MGGCHHCDYR GVFQAEGDGQ KCLTGCGEPS QRYYHVPRSF LKNGEPNTLI 

       730        740        750        760        770        780 
LFEEAGGDPS QVIFHSVVAG SVCVSAEVGD AITLSCGQHS KTISTIDVTS FGVARGQCGA 

       790        800        810        820 
YEGGCESKAA YKAFTEACLG KESCTVQIIN ALTGSGCLSG VLTVQASC 

« Hide

References

« Hide 'large scale' references
[1]"In-depth view of structure, activity, and evolution of rice chromosome 10."
Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. expand/collapse author list , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.
Science 300:1566-1569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[5]"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
The rice full-length cDNA consortium
Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC091749 Genomic DNA. Translation: AAL31090.1. Different initiation.
AC131374 Genomic DNA. Translation: AAN04162.1. Different initiation.
DP000086 Genomic DNA. Translation: AAP53027.2.
AP008216 Genomic DNA. Translation: BAF26280.1.
CM000147 Genomic DNA. Translation: EAZ15685.1. Different initiation.
AK119350 mRNA. No translation available.
RefSeqNP_001064366.1. NM_001070901.1.
UniGeneOs.46702.

3D structure databases

ProteinModelPortalQ7G3T8.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH35. Glycoside Hydrolase Family 35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsOS10T0330600-01; OS10T0330600-01; OS10G0330600.
GeneID4348337.
KEGGosa:4348337.

Organism-specific databases

GrameneQ7G3T8.

Phylogenomic databases

eggNOGCOG1874.
HOGENOMHOG000239919.
OMAFQTVTVG.
ProtClustDBCLSN2691488.

Gene expression databases

ArrayExpressQ7G3T8.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
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.
IPR000922. Lectin_gal-bd_dom.
[Graphical view]
PANTHERPTHR23421. PTHR23421. 1 hit.
PfamPF02140. Gal_Lectin. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]
PRINTSPR00742. GLHYDRLASE35.
SUPFAMSSF49785. SSF49785. 3 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS01182. GLYCOSYL_HYDROL_F35. 1 hit.
PS50228. SUEL_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGA13_ORYSJ
AccessionPrimary (citable) accession number: Q7G3T8
Secondary accession number(s): A3C3M2, Q7G642, Q8W5D6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: August 22, 2006
Last modified: November 13, 2013
This is version 58 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

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries