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Q7G764 (NADO1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable NAD(P)H-dependent oxidoreductase 1

EC=1.1.1.-
Gene names
Ordered Locus Names:Os10g0113000, LOC_Os10g02380
ORF Names:OJ1014H12.13, OSJNBb0012A20.18
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in auxin-induced cell growth by generating hydroxyl radicals, which tends to increase cell wall loosening. Ref.5

Tissue specificity

Expressed in roots and leaf sheaths. Ref.5

Induction

By auxin and gibberellic acid. Ref.5

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321Probable NAD(P)H-dependent oxidoreductase 1
PRO_0000124655

Regions

Nucleotide binding214 – 27360NADP By similarity

Sites

Active site551Proton donor By similarity
Binding site1181Substrate By similarity
Site851Lowers pKa of active site Tyr By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7G764 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2B7906FED1FFCC34

FASTA32135,713
        10         20         30         40         50         60 
MATIPEVPAS ELIQTMPRVG MGTAAFPFTS SEDTTAAMLR AIELGYRHFD TARIYATEGC 

        70         80         90        100        110        120 
VGEAVAEAVR RGLIASRADV FVTSKIWCSD LHAGRVVPAA RETLRNLGMD YVDLLLVHWP 

       130        140        150        160        170        180 
VSLTPGNYDF PFPKEVILPS FDMEGVWRGM EECHRLGLAR AIGVSNFSAK KLEQLLSLAA 

       190        200        210        220        230        240 
VRPAVNQVEV NPMWQQRTLR EVCRREGVQL CGYSPLGAKG TPWGSAAVMD SGVLQEIAGA 

       250        260        270        280        290        300 
KGKTLAQICL RWLYEQGDVL LVKTYNEKRM KENLDIFNWE LTDEERERIS QLPQLRGLPG 

       310        320 
LEFISDHGPY KSVEDLWDGD V 

« 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: 12791992] [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: 16100779] [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: 18089549] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"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: 12869764] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.
[5]"Characterization of NADPH-dependent oxidoreductase induced by auxin in rice."
Oguchi K., Tanaka N., Komatsu S., Akao S.
Physiol. Plantarum 121:124-131(2004) [PubMed: 15086826] [Abstract]
Cited for: PROTEIN SEQUENCE OF 12-21; 68-76; 153-162 AND 237-256, FUNCTION, INDUCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC079685 Genomic DNA. Translation: AAK52587.1.
AC098694 Genomic DNA. Translation: AAM44874.1.
DP000086 Genomic DNA. Translation: AAP51850.1.
AP008216 Genomic DNA. Translation: BAF25957.1.
AK061106 mRNA. No translation available.
AK102609 mRNA. No translation available.
RefSeqNP_001064043.1. NM_001070578.1.
UniGeneOs.4020.

3D structure databases

ProteinModelPortalQ7G764.
ModBaseSearch...

Proteomic databases

PRIDEQ7G764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4347977.
KEGGosa:4347977.
NMPDRfig|39947.1.peg.11110.

Organism-specific databases

GrameneQ7G764.

Phylogenomic databases

HOGENOMHBG605727.
PhylomeDBQ7G764.
ProtClustDBCLSN2697974.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFPIRSF000097. AKR. 1 hit.
PRINTSPR00069. ALDKETRDTASE.
SUPFAMSSF51430. Aldo/ket_red. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNADO1_ORYSJ
AccessionPrimary (citable) accession number: Q7G764
Secondary accession number(s): Q0IZA8, Q94LH9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: July 5, 2004
Last modified: December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families