Q56YU0 (AL2C4_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 58.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Aldehyde dehydrogenase family 2 member C4 EC=1.2.1.3 Alternative name(s): ALDH1a Protein REDUCED EPIDERMAL FLUORESCENCE 1 | ||||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 501 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Involved in ferulic acid and sinapic acid biosynthesis by oxidation of conyferylaldehyde and sinapaldehyde, respectively. Can oxidize L-lactaldehyde. Possesses activity on acetaldehyde and glycolaldehyde in vitro. Ref.1 Ref.6 |
| Catalytic activity | An aldehyde + NAD+ + H2O = a carboxylate + NADH. |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | |
| Post-translational modification | Ubiquitinated. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Ubl conjugation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | phenylpropanoid biosynthetic process Inferred from direct assay Ref.6. Source: TAIR |
| Cellular_component | cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | aldehyde dehydrogenase (NAD) activity Inferred from sequence or structural similarity Ref.1. Source: TAIR coniferyl-aldehyde dehydrogenase activityInferred from direct assay Ref.6. Source: TAIR |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 501 | 501 | Aldehyde dehydrogenase family 2 member C4 | PRO_0000256058 | |||||
Regions | |||||||||
| Nucleotide binding | 245 – 250 | 6 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 268 | 1 | Proton acceptor By similarity | ||||||
| Active site | 302 | 1 | Nucleophile By similarity | ||||||
| Site | 169 | 1 | Transition state stabilizer By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 152 | 1 | G → E in ref1-7; reduced activity on sinapaldehyde. Ref.6 | ||||||
| Mutagenesis | 416 | 1 | G → R in ref1-6; reduced activity on sinapaldehyde. Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of the aldehyde dehydrogenase gene families of Zea mays and Arabidopsis." Skibbe D.S., Liu F., Wen T.-J., Yandeau M.D., Cui X., Cao J., Simmons C.R., Schnable P.S. Plant Mol. Biol. 48:751-764(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. |
| [2] | "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(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. 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. Shinozaki K.Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 322-501. Strain: cv. Columbia. |
| [6] | "The Arabidopsis thaliana REDUCED EPIDERMAL FLUORESCENCE1 gene encodes an aldehyde dehydrogenase involved in ferulic acid and sinapic acid biosynthesis." Nair R.B., Bastress K.L., Ruegger M.O., Denault J.W., Chapple C. Plant Cell 16:544-554(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-152 AND GLY-416. |
| [7] | "The ALDH gene superfamily of Arabidopsis." Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J. Trends Plant Sci. 9:371-377(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE. |
| [8] | "Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis." Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D. Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF349448 mRNA. Translation: AAM27004.1. AB020746 Genomic DNA. Translation: BAB01998.1. CP002686 Genomic DNA. Translation: AEE76907.1. AY056398 mRNA. Translation: AAL08254.1. AK221230 mRNA. Translation: BAD93825.1. |
| IPI | IPI00543086. |
| RefSeq | NP_566749.1. NM_113359.3. |
| UniGene | At.22894. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ZUM based on UniProtKB P05091. |
| ProteinModelPortal | Q56YU0. |
| SMR | Q56YU0. Positions 15-485. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q56YU0. 1 interaction. |
| STRING | 3702.AT3G24503.1-P. |
Proteomic databases | |
| PaxDb | Q56YU0. |
| PRIDE | Q56YU0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT3G24503.1; AT3G24503.1; AT3G24503. |
| GeneID | 822042. |
| KEGG | ath:AT3G24503. |
Organism-specific databases | |
| TAIR | At3g24503. |
Phylogenomic databases | |
| eggNOG | COG1012. |
| HOGENOM | HOG000271505. |
| InParanoid | Q56YU0. |
| KO | K12355. |
| OMA | EPFMAEV. |
| PhylomeDB | Q56YU0. |
| ProtClustDB | PLN02766. |
Gene expression databases | |
| Genevestigator | Q56YU0. |
Family and domain databases | |
| Gene3D | 3.40.309.10. 1 hit. 3.40.605.10. 1 hit. |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view] |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AL2C4_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q56YU0 Secondary accession number(s): Q9LV57 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
