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P25795 (AL7A1_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Aldehyde dehydrogenase family 7 member A1

EC=1.2.1.3
Alternative name(s):
Antiquitin-1
Turgor-responsive protein 26G
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Subunit structure

Homotetramer By similarity.

Induction

By dehydration of shoots but not roots and not by heat shock or ABA.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Biological processStress response
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processresponse to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 508507Aldehyde dehydrogenase family 7 member A1
PRO_0000056498

Regions

Nucleotide binding244 – 2496NAD By similarity

Sites

Active site2661Proton acceptor By similarity
Active site3001Nucleophile By similarity
Site1651Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P25795 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CC88F367B52E923D

FASTA50853,789
        10         20         30         40         50         60 
MGSDSNNLGF LKEIGLGATN IGSFINGQWK ANGPTVHSVN PSTNQVIASV TEATLDDYEE 

        70         80         90        100        110        120 
GLRASSEAAK TWRTVPAPKR GEIVRQIGDA LRAKLDPLGR LVALEMGKIL AEGIGEVQEI 

       130        140        150        160        170        180 
IDMCDYSVGL SRQLNGSIIP SERPEHMMFE VWNPLGIVGV ITAFNFPCAV LGWNACIALV 

       190        200        210        220        230        240 
GGNTVVWKGA PTTPLITVAV TKLIAEVFER NNLPGAIFTA LCGGADIGHA IAKDTRIPLV 

       250        260        270        280        290        300 
SFTGSSKVGA LVQQTVSQRF GKTLLELSGN NAIIVMDDAD ITLAVRSIFF AAVGTAGQRC 

       310        320        330        340        350        360 
TTCRRLYLHE SVYANVLEQL TALYKQVKIG NPLEEGTLVG PLHTRSAVEN FKNGISAIKS 

       370        380        390        400        410        420 
QGGKIVTGGS VLESEGNFVV PTIVEISADA AVVKEELFAP VLYVMKFKDL EEAIALNNSV 

       430        440        450        460        470        480 
PQGLSSSIFT QKPSTIFKWI GPSGSDCGIV NVNIPTNGAE IGGAFGGEKA TGGGREAGSD 

       490        500 
SWKQYMRRST CTINYGSELP LAQGINFG 

« Hide

References

[1]"Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes."
Guerrero F.D., Jones J.T., Mullet J.E.
Plant Mol. Biol. 15:11-26(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Progress No. 9.
[2]"First purification of the antiquitin protein and demonstration of its enzymatic activity."
Tang W.-K., Cheng C.H.K., Fong W.-P.
FEBS Lett. 516:183-186(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54359 mRNA. Translation: CAA38243.1.
PIRS11863.

3D structure databases

ProteinModelPortalP25795.
SMRP25795. Positions 10-507.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP25795.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAL7A1_PEA
AccessionPrimary (citable) accession number: P25795
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 74 of the entry and version 3 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