[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Progress No. 9; DOI=10.1007/BF00017720; PubMed=1715781 [NCBI, ExPASy, EBI, Israel, Japan] Guerrero F.D., Jones J.T., Mullet J.E.; "Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes."; Plant Mol. Biol. 15:11-26(1990).
[2]	PROTEIN SEQUENCE OF 2-16. DOI=10.1016/S0014-5793(02)02553-X; PubMed=11959129 [NCBI, ExPASy, EBI, Israel, Japan] Tang W.-K., Cheng C.H.K., Fong W.-P.; "First purification of the antiquitin protein and demonstration of its enzymatic activity."; FEBS Lett. 516:183-186(2002).

Comments

CATALYTIC ACTIVITY: An aldehyde + NAD⁺ + H₂O = an acid + NADH.
SUBUNIT: Homotetramer (By similarity).
INDUCTION: By dehydration of shoots but not roots and not by heat shock or ABA.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X54359; CAA38243.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S11863; S11863.

3D structure databases

HSSP

P51977; 1BXS. [HSSP ENTRY / PDB]

ModBase

P25795.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; NAD; Oxidoreductase; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 508`	`507`	`Aldehyde dehydrogenase family 7 member A1.`	`PRO_0000056498`
`NP_BIND`	`244 249`	`6`	`NAD (By similarity).`
`ACT_SITE`	`266 266`		`Proton acceptor (By similarity).`
`ACT_SITE`	`300 300`		`Nucleophile (By similarity).`
`SITE`	`165 165`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 508 AA [This is the length of the unprocessed precursor]

Molecular weight: 53789 Da [This is the MW of the unprocessed precursor]

CRC64: CC88F367B52E923D [This is a checksum on the sequence]

        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

P25795 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools