Reviewed, UniProtKB/Swiss-Prot P06525 (ADH1_ARATH)

Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase class-P
    EC=1.1.1.1

Gene names

Name:	ADH1
Synonyms:	ADH
Ordered Locus Names:	At1g77120
ORF Names:	F22K20.19

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH.
Cofactor	Binds 2 zinc ions per subunit.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Induction	By 2,4-dichlorophenoxyacetic acid in Arabidopsis as well as in maize.
Miscellaneous	Unlike most plants, Arabidopsis contains only one gene for ADH.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-P subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ion Inferred from expression pattern. Source: TAIR response to hypoxia Inferred from expression pattern. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR
Cellular component	cytosol Ref.12 Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	alcohol dehydrogenase (NAD) activity Ref.11 Inferred from mutant phenotype. Source: TAIR zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 379	379	Alcohol dehydrogenase class-P		PRO_0000160697
Regions
	Nucleotide binding	202 – 207	6	NAD By similarity
	Nucleotide binding	295 – 297	3	NAD By similarity
Sites
	Metal binding	47	1	Zinc 1; catalytic By similarity
	Metal binding	69	1	Zinc 1; catalytic By similarity
	Metal binding	99	1	Zinc 2 By similarity
	Metal binding	102	1	Zinc 2 By similarity
	Metal binding	105	1	Zinc 2 By similarity
	Metal binding	113	1	Zinc 2 By similarity
	Metal binding	177	1	Zinc 1; catalytic By similarity
	Binding site	226	1	NAD By similarity
	Binding site	231	1	NAD By similarity
	Binding site	372	1	NAD By similarity
Amino acid modifications
	Modified residue	229	1	Phosphoserine Ref.12 Ref.13
Natural variations
	Natural variant	43	1	F → Y in strain: cv. Hiroshima.
	Natural variant	51	1	V → L in strain: cv. Bla-10, cv. Ci-0, cv. Cvi-0, cv. Hiroshima, cv. Kas-1 and cv. Ita-0.
	Natural variant	101	1	E → D in strain: cv. Aa-0, cv. Al-0, cv. Bl-1, cv. Bs-0, cv. Gr-1, cv. Mt-0, cv. Shokei and cv. Yo-0. Ref.10
	Natural variant	106	1	H → K in strain: cv. Bl-1 and cv. Gr-1. Ref.10
	Natural variant	106	1	H → Q in strain: cv. Aa-0, cv. Al-0, cv. Bs-0, cv. Mt-0, cv. Shokei and cv. Yo-0.
	Natural variant	120	1	T → P in strain: cv. Es-0.
	Natural variant	180	1	S → A in strain: cv. Bla-10.
	Natural variant	197	1	S → T in strain: cv. Cvi-0.
	Natural variant	217	1	A → V in strain: cv. Kas-1.
Experimental info
	Mutagenesis	105	1	C → Y in R006; inactive enzyme.
	Sequence conflict	154	1	V → L in AAM65556. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P06525-1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: 32550529538B9669	FASTA	379	41,178
	10 20 30 40 50 60 MSTTGQIIRC KAAVAWEAGK PLVIEEVEVA PPQKHEVRIK ILFTSLCHTD VYFWEAKGQT 70 80 90 100 110 120 PLFPRIFGHE AGGIVESVGE GVTDLQPGDH VLPIFTGECG ECRHCHSEES NMCDLLRINT 130 140 150 160 170 180 ERGGMIHDGE SRFSINGKPI YHFLGTSTFS EYTVVHSGQV AKINPDAPLD KVCIVSCGLS 190 200 210 220 230 240 TGLGATLNVA KPKKGQSVAI FGLGAVGLGA AEGARIAGAS RIIGVDFNSK RFDQAKEFGV 250 260 270 280 290 300 TECVNPKDHD KPIQQVIAEM TDGGVDRSVE CTGSVQAMIQ AFECVHDGWG VAVLVGVPSK 310 320 330 340 350 360 DDAFKTHPMN FLNERTLKGT FFGNYKPKTD IPGVVEKYMN KELELEKFIT HTVPFSEINK 370 AFDYMLKGES IRCIITMGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and DNA sequence of the Arabidopsis thaliana alcohol dehydrogenase gene." Chang C., Meyerowitz E.M. Proc. Natl. Acad. Sci. U.S.A. 83:1408-1412(1986) [PubMed: 2937058] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Haplotypic divergence coupled with lack of diversity at the Arabidopsis thaliana alcohol dehydrogenase locus: roles for both balancing and directional selection?" Hanfstingl U., Berry A., Kellogg E.A., Costa J.T. III, Ruediger W., Ausubel F.M. Genetics 138:811-828(1994) [PubMed: 7851777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Intragenic recombination in the Adh locus of the wild plant Arabidopsis thaliana." Innan H., Tajima F., Terauchi R., Miyashita N.T. Genetics 143:1761-1770(1996) [PubMed: 8844162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Al-0, cv. Bl-1, cv. Bla-10, cv. Bs-0, cv. Chi-0, cv. Ci-0, cv. Es-0, cv. Gr-1, cv. Ita-0 and cv. Yo-0.
[4]	"Intra- and interspecific variation of the alcohol dehydrogenase locus region in wild plants Arabis gemmifera and Arabidopsis thaliana." Miyashita N.T., Innan H., Terauchi R. Mol. Biol. Evol. 13:433-436(1996) [PubMed: 8587508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Aa-0, cv. Hiroshima, cv. Mt-0, cv. Pog-0 and cv. Shokei.
[5]	"Comparative evolutionary analysis of chalcone synthase and alcohol dehydrogenase loci in Arabidopsis, Arabis, and related genera (Brassicaceae)." Koch M.A., Haubold B., Mitchell-Olds T. Mol. Biol. Evol. 17:1483-1498(2000) [PubMed: 11018155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"DNA variation in the 5' upstream region of the Adh locus of the wild plants Arabidopsis thaliana and Arabis gemmifera." Miyashita N.T. Mol. Biol. Evol. 18:164-171(2001) [PubMed: 11158375] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Cvi-0 and cv. Kas-1.
[7]	"Post-transcriptional silencing of the Arabidopsis adh1 gene triggered by a fully homologous transgene." Santos D. Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. C24.
[8]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[9]	"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. , 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.
[10]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASP-101 AND LYS-106.
[11]	"Sequence analysis of two null-mutant alleles of the single Arabidopsis Adh locus." Dolferus R., van den Bossche D., Jacobs M. Mol. Gen. Genet. 224:297-302(1990) [PubMed: 2277648] [Abstract] Cited for: MUTANT R006.
[12]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed: 18433157] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, MASS SPECTROMETRY.
[13]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed: 19245862] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12196 Genomic DNA. Translation: AAA32728.1. X77943 Genomic DNA. Translation: CAA54911.1. D84240 Genomic DNA. Translation: BAA19615.1. D84241 Genomic DNA. Translation: BAA19616.1. D84242 Genomic DNA. Translation: BAA19617.1. D84243 Genomic DNA. Translation: BAA19618.1. D84244 Genomic DNA. Translation: BAA19619.1. D84245 Genomic DNA. Translation: BAA19620.1. D84246 Genomic DNA. Translation: BAA19621.1. D84247 Genomic DNA. Translation: BAA19622.1. D84248 Genomic DNA. Translation: BAA19623.1. D84249 Genomic DNA. Translation: BAA19624.1. D63460 Genomic DNA. Translation: BAA22983.1. D63461 Genomic DNA. Translation: BAA22979.1. D63462 Genomic DNA. Translation: BAA22980.1. D63463 Genomic DNA. Translation: BAA22981.1. D63464 Genomic DNA. Translation: BAA22982.1. AF110456 Genomic DNA. Translation: AAF23554.1. AB048394 Genomic DNA. Translation: BAB32568.1. AB048395 Genomic DNA. Translation: BAB32569.1. AY536888 Genomic DNA. Translation: AAS45601.2. AC002291 Genomic DNA. Translation: AAC00625.1. AY045612 mRNA. Translation: AAK73970.1. AY090330 mRNA. Translation: AAL90991.1. AY088010 mRNA. Translation: AAM65556.1.
IPI	IPI00539119.
PIR	DEMUAM. A23815.
RefSeq	NP_177837.1.
UniGene	At.22653 At.64099 Rra.8365
3D structure databases
SMR	P06525. Positions 5-377.
ModBase	Search...
Proteomic databases
PRIDE	P06525.
Genome annotation databases
GeneID	844047.
GenomeReviews	Gene locus AT1G77120 in contig CT485782_GR.
KEGG	ath:AT1G77120.
NMPDR	fig|3702.1.peg.7251.
Organism-specific databases
TAIR	At1g77120.
Phylogenomic databases
InParanoid	P06525.
OMA	NANRFEE.
PhylomeDB	P06525.
Enzyme and pathway databases
BRENDA	1.1.1.1. 302.
Gene expression databases
ArrayExpress	P06525.
Genevestigator	P06525.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADH1_ARATH

Accession

Primary (citable) accession number: P06525
Secondary accession number(s): O04080 , O04713, O04717, O04868, O23821, Q8LA61, Q94AY6, Q9CAZ2, Q9CAZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	May 29, 2007
Last modified:	February 9, 2010
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)