Q96533 (ADHX_ARATH) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › 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: KM=1.4 µM for S-(hydroxymethyl)glutathione Vmax=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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ethanol oxidation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	S-(hydroxymethyl)glutathione dehydrogenase activity Inferred from electronic annotation. Source: EC 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

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

Experimental info

Sequence conflict

84

1

E → G in AAB06322. Ref.1

Sequence conflict

354

1

T → S in CAA57973. Ref.2

Secondary structure

1

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379

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Beta strand

23 – 29

7

Beta strand

36 – 46

11

Helix

48 – 54

7

Beta strand

63 – 65

3

Beta strand

70 – 78

9

Beta strand

90 – 93

4

Beta strand

100 – 102

3

Helix

103 – 107

5

Helix

117 – 120

4

Turn

121 – 123

3

Turn

126 – 128

3

Beta strand

132 – 135

4

Beta strand

138 – 141

4

Turn

144 – 146

3

Beta strand

149 – 156

8

Helix

157 – 159

3

Beta strand

160 – 162

3

Helix

169 – 172

4

Helix

173 – 176

4

Helix

178 – 187

10

Turn

188 – 190

3

Beta strand

198 – 201

4

Helix

205 – 217

13

Beta strand

222 – 225

4

Helix

231 – 236

6

Turn

237 – 239

3

Beta strand

242 – 244

3

Helix

246 – 248

3

Helix

253 – 260

8

Beta strand

265 – 270

6

Helix

275 – 283

9

Turn

287 – 289

3

Beta strand

291 – 294

4

Beta strand

304 – 306

3

Helix

309 – 312

4

Beta strand

316 – 319

4

Helix

322 – 324

3

Helix

327 – 339

13

Helix

346 – 348

3

Beta strand

349 – 354

6

Helix

355 – 357

3

Helix

358 – 364

7

Beta strand

371 – 376

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 27, 2002. Version 2. Checksum: 045054298F16B258	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. , 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] [Europe PMC] [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. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., 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] [Europe PMC] [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] [Europe PMC] [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

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3UKO	X-ray	1.40	A/B	2-379	[»]
4GL4	X-ray	1.80	A/B	2-379	[»]

ProteinModelPortal

Q96533.

SMR

Q96533. Positions 2-379.

ModBase

Search...

Proteomic databases

PaxDb

Q96533.

PRIDE

Q96533.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT5G43940.1; AT5G43940.1; AT5G43940.

GeneID

834417.

KEGG

ath:AT5G43940.

Organism-specific databases

TAIR

At5g43940.

Phylogenomic databases

eggNOG

COG1062.

HOGENOM

HOG000294674.

InParanoid

Q96533.

KO

K00121.

PhylomeDB

Q96533.

ProtClustDB

CLSN2686871.

Gene expression databases

ArrayExpress

Q96533.

Genevestigator

Q96533.

GermOnline

AT5G43940. Arabidopsis thaliana.

Family and domain databases

Gene3D

3.40.50.720. 1 hit.

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]

PANTHER

PTHR11695. PTHR11695. 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:	May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program