Alcohol dehydrogenase class-3 - Arabidopsis thaliana (Mouse-ear cress)

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Q96533 (ADHX_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alcohol dehydrogenase class-3
EC=1.1.1.1

Alternative name(s):
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase
Short name=FALDH
Short name=FDH
Short name=GSH-FDH
EC=1.1.1.-
S-(hydroxymethyl)glutathione dehydrogenase
EC=1.1.1.284

Gene names

Name:	ADH2
Synonyms:	ADHIII, FDH1
Ordered Locus Names:	At5g43940
ORF Names:	MRH10.4

Organism

Arabidopsis thaliana (Mouse-ear cress)

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

General annotation (Comments)

Function	Plays a central role in formaldehyde detoxification. Ref.9
Catalytic activity	An alcohol + NAD⁺ = an aldehyde or ketone + NADH. Ref.2 S-(hydroxymethyl)glutathione + NAD(P)⁺ = S-formylglutathione + NAD(P)H. Ref.2
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Potential.
Tissue specificity	Ubiquitous. Ref.2
Induction	Down-regulated by wounding and activated by salicylic acid (SA). Ref.8
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=1.4 µM for S-(hydroxymethyl)glutathione V_max=1.22 µmol/min/mg enzyme

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell death Inferred from mutant phenotype. Source: TAIR ethanol oxidation Inferred from electronic annotation. Source: InterPro formaldehyde metabolic process Inferred from direct assay Ref.2. Source: TAIR heat acclimation Inferred from mutant phenotype. Source: TAIR seed development Inferred from mutant phenotype. Source: TAIR
Cellular component	cytosol Inferred from direct assay. Source: TAIR peroxisome Inferred from direct assay. Source: TAIR
Molecular function	S-(hydroxymethyl)glutathione dehydrogenase activity Inferred from direct assay Ref.9. Source: TAIR S-nitrosoglutathione reductase activity Inferred from mutant phenotype. Source: TAIR alcohol dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select] Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q96533-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Alcohol dehydrogenase class-3

PRO_0000160771

Sites

Metal binding

Zinc 1; catalytic By similarity

Metal binding

Zinc 1; catalytic By similarity

Metal binding

Zinc 2 By similarity

Metal binding

102

Zinc 2 By similarity

Metal binding

105

Zinc 2 By similarity

Metal binding

113

Zinc 2 By similarity

Metal binding

177

Zinc 1; catalytic By similarity

Experimental info

Sequence conflict

E → G in AAB06322. Ref.1

Sequence conflict

354

T → S in CAA57973. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Isoform 1 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: 045054298F16B258
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FASTA

379

40,699

        10         20         30         40         50         60 
MATQGQVITC KAAVAYEPNK PLVIEDVQVA PPQAGEVRIK ILYTALCHTD AYTWSGKDPE 

        70         80         90        100        110        120 
GLFPCILGHE AAGIVESVGE GVTEVQAGDH VIPCYQAECR ECKFCKSGKT NLCGKVRSAT 

       130        140        150        160        170        180 
GVGIMMNDRK SRFSVNGKPI YHFMGTSTFS QYTVVHDVSV AKIDPTAPLD KVCLLGCGVP 

       190        200        210        220        230        240 
TGLGAVWNTA KVEPGSNVAI FGLGTVGLAV AEGAKTAGAS RIIGIDIDSK KYETAKKFGV 

       250        260        270        280        290        300 
NEFVNPKDHD KPIQEVIVDL TDGGVDYSFE CIGNVSVMRA ALECCHKGWG TSVIVGVAAS 

       310        320        330        340        350        360 
GQEISTRPFQ LVTGRVWKGT AFGGFKSRTQ VPWLVEKYMN KEIKVDEYIT HNLTLGEINK 

       370 
AFDLLHEGTC LRCVLDTSK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the Arabidopsis and rice formaldehyde dehydrogenase genes: implications for the origin of plant ADH enzymes." Dolferus R., Osterman J.C., Peacock W.J., Dennis E.S. Genetics 146:1131-1141(1997) [PubMed: 9215914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. C24.
[2]	"Arabidopsis formaldehyde dehydrogenase. Molecular properties of plant class III alcohol dehydrogenase provide further insights into the origins, structure and function of plant class P and liver class I alcohol dehydrogenases." Martinez M.C., Achkor H., Persson B., Fernandez M.R., Shafqat J., Farres J., Joernvall H., Pares X. Eur. J. Biochem. 241:849-857(1996) [PubMed: 8944774] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, ENZYME ACTIVITY. Strain: cv. Landsberg erecta. Tissue: Flower.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones." Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:291-300(1997) [PubMed: 9405937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"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 (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[7]	"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].
[8]	"The gene encoding glutathione-dependent formaldehyde dehydrogenase/GSNO reductase is responsive to wounding, jasmonic acid and salicylic acid." Diaz M., Achkor H., Titarenko E., Martinez M.C. FEBS Lett. 543:136-139(2003) [PubMed: 12753920] [Abstract] Cited for: INDUCTION.
[9]	"Enhanced formaldehyde detoxification by overexpression of glutathione-dependent formaldehyde dehydrogenase from Arabidopsis." Achkor H., Diaz M., Fernandez M.R., Biosca J.A., Pares X., Martinez M.C. Plant Physiol. 132:2248-2255(2003) [PubMed: 12913179] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U63931 Genomic DNA. Translation: AAB06322.1. X82647 mRNA. Translation: CAA57973.1. AB006703 Genomic DNA. Translation: BAB09054.1. CP002688 Genomic DNA. Translation: AED95034.1. AY039601 mRNA. Translation: AAK62656.1. BT010169 mRNA. Translation: AAQ22638.1. AK226412 mRNA. Translation: BAE98557.1. AY087250 mRNA. Translation: AAM64806.1.
IPI	IPI00527514.
PIR	S71244.
RefSeq	NP_199207.1. NM_123761.3.
UniGene	At.23457. At.63885.
3D structure databases
ProteinModelPortal	Q96533.
SMR	Q96533. Positions 6-375.
ModBase	Search...
Protein-protein interaction databases
STRING	Q96533.
Proteomic databases
PRIDE	Q96533.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G43940.1; AT5G43940.1; AT5G43940.
GeneID	834417.
GenomeReviews	Gene locus AT5G43940 in contig BA000015_GR.
KEGG	ath:AT5G43940.
NMPDR	fig\|3702.1.peg.26142.
Organism-specific databases
TAIR	At5g43940.
Phylogenomic databases
GeneTree	EPGT00050000000862.
HOGENOM	HBG753318.
InParanoid	Q96533.
OMA	EFGASEC.
PhylomeDB	Q96533.
ProtClustDB	CLSN2686871.
Gene expression databases
ArrayExpress	Q96533.
Genevestigator	Q96533.
GermOnline	AT5G43940. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR014183. ADH_3. IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00121.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 2 hits.
TIGRFAMs	TIGR02818. Adh_III_F_hyde. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADHX_ARATH

Accession

Primary (citable) accession number: Q96533
Secondary accession number(s): Q0WWE1, Q43384, Q9FND2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 27, 2002
Last modified:	December 14, 2011
This is version 103 of the entry and version 2 of the sequence. [Complete history]

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

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents