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Reviewed, UniProtKB/Swiss-Prot Q56YU0 (AL2C4_ARATH)

Last modified June 16, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aldehyde dehydrogenase family 2 member C4
    EC=1.2.1.3
Alternative name(s):
    ALDH1a
    Protein REDUCED EPIDERMAL FLUORESCENCE 1
Gene names
Name: ALDH2C4
Synonyms: REF1
Ordered Locus Names: At3g24503
ORF Names: MOB24.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.5

Catalytic activity

An aldehyde + NAD+ + H2O = an acid + NADH.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasmcytosol Potential.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

phenylpropanoid biosynthetic process Ref.5

Inferred from direct assay. Source: TAIR

   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

coniferyl-aldehyde dehydrogenase activity Ref.5

Inferred from direct assay. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Aldehyde dehydrogenase family 2 member C4
PRO_0000256058

Regions

Nucleotide binding245 – 2506NAD By similarity

Sites

Active site2681Proton acceptor By similarity
Active site3021Nucleophile By similarity
Site1691Transition state stabilizer By similarity

Experimental info

Mutagenesis1521G → E in ref1-7; reduced activity on sinapaldehyde. Ref.5
Mutagenesis4161G → R in ref1-6; reduced activity on sinapaldehyde. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q56YU0-1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 3E93A166B1D3ECF6

FASTA50154,360
        10         20         30         40         50         60 
MENGKCNGAT TVKLPEIKFT KLFINGQFID AASGKTFETI DPRNGEVIAT IAEGDKEDVD 

        70         80         90        100        110        120 
LAVNAARYAF DHGPWPRMTG FERAKLINKF ADLIEENIEE LAKLDAVDGG KLFQLGKYAD 

       130        140        150        160        170        180 
IPATAGHFRY NAGAADKIHG ETLKMTRQSL FGYTLKEPIG VVGNIIPWNF PSIMFATKVA 

       190        200        210        220        230        240 
PAMAAGCTMV VKPAEQTSLS ALFYAHLSKE AGIPDGVLNI VTGFGSTAGA AIASHMDVDK 

       250        260        270        280        290        300 
VSFTGSTDVG RKIMQAAAAS NLKKVSLELG GKSPLLIFND ADIDKAADLA LLGCFYNKGE 

       310        320        330        340        350        360 
ICVASSRVFV QEGIYDKVVE KLVEKAKDWT VGDPFDSTAR QGPQVDKRQF EKILSYIEHG 

       370        380        390        400        410        420 
KNEGATLLTG GKAIGDKGYF IQPTIFADVT EDMKIYQDEI FGPVMSLMKF KTVEEGIKCA 

       430        440        450        460        470        480 
NNTKYGLAAG ILSQDIDLIN TVSRSIKAGI IWVNCYFGFD LDCPYGGYKM SGNCRESGMD 

       490        500 
ALDNYLQTKS VVMPLHNSPW M 

« Hide

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: 11999848] [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: 10907853] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"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: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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 322-501.
Strain: cv. Columbia.
[5]"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: 14729911] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-152 AND GLY-416.
[6]"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: 15358267] [Abstract]
Cited for: NOMENCLATURE.

Cross-references

Sequence databases

AF349448 mRNA. Translation: AAM27004.1.
AB020746 Genomic DNA. Translation: BAB01998.1.
AY056398 mRNA. Translation: AAL08254.1.
AK221230 mRNA. Translation: BAD93825.1.
IPIIPI00543086.
RefSeqNP_566749.1.
UniGeneAt.22894

3D structure databases

HSSPHSSP built from PDB template 1O04 based on UniProtKB P05091.
ModBaseSearch...

Proteomic databases

PRIDEQ56YU0.
ProMEXQ56YU0.

Genome annotation databases

GeneID822042.
GenomeReviewsGene locus AT3G24503 in contig BA000014_GR.
KEGGath:AT3G24503.
NMPDRfig|3702.1.peg.14712.

Organism-specific databases

TAIRAt3g24503.

Phylogenomic databases

OMAQ56YU0. SALFYAH.

Enzyme and pathway databases

BRENDA1.2.1.3. 302.

Family and domain databases

InterProIPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHERPTHR11699. Aldehyde_dehyd. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAL2C4_ARATH
AccessionPrimary (citable) accession number: Q56YU0
Secondary accession number(s): Q9LV57
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: June 16, 2009
This is version 27 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents