P80572 (ADHX_PEA) 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
Organism	Pisum sativum (Garden pea)
Taxonomic identifier	3888 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	378 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH. S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 378	378	Alcohol dehydrogenase class-3		PRO_0000160774
Sites
	Metal binding	46	1	Zinc 1; catalytic By similarity
	Metal binding	68	1	Zinc 1; catalytic By similarity
	Metal binding	98	1	Zinc 2 By similarity
	Metal binding	101	1	Zinc 2 By similarity
	Metal binding	104	1	Zinc 2 By similarity
	Metal binding	112	1	Zinc 2 By similarity
	Metal binding	176	1	Zinc 1; catalytic By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylalanine Ref.1 Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P80572 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: 9ED1C511219FF45B	FASTA	378	40,489
	10 20 30 40 50 60 ATQGQVITCK AAVAWEPNKP LTIEDVEVAP PQANEVRIQI LFTALCHTDA YTLGGKDPEG 70 80 90 100 110 120 LFPCILGHEA AGIVESVGEG VTDVKPGDHV IPSYQAECGE CKFCKSPKTN LCGKVRAATG 130 140 150 160 170 180 VGVMMADRKS RFSVKGKPIY HFMGTSTFSQ YTVVHDVSVA KIHPDAPLDK VCLLGCGVPT 190 200 210 220 230 240 GLGAVWNTAK VEPGSIVAIF GLGTVGLAVA EGAKSAGASR IIGIDIDSNK YDTAKNFGVT 250 260 270 280 290 300 EFINPKDHEK PIQQVIIDLT DGGVDYSFEC LGNVSVMRSA LECCHKGWGT SVIVGVAASG 310 320 330 340 350 360 QEISTRPFQL VTGRVWKGTA FGGFKSRSQV PWLVEKYLKK EIKVDEYITH NLTLLEINKA 370 FDLLHEGQCL RCVLAVHD

References

[1]	"Pea formaldehyde-active class III alcohol dehydrogenase: common derivation of the plant and animal forms but not of the corresponding ethanol-active forms (classes I and P)." Shafqat J., El-Ahmad M., Danielsson O., Martinez M.C., Persson B., Pares X., Joernvall H. Proc. Natl. Acad. Sci. U.S.A. 93:5595-5599(1996) [PubMed: 8643621] [Abstract] Cited for: PROTEIN SEQUENCE, ACETYLATION AT ALA-1.
[2]	"Multiplicity of N-terminal structures of medium-chain alcohol dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme." Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J., Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Joernvall H. FEBS Lett. 367:237-240(1995) [PubMed: 7607314] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	S66198.
3D structure databases
ProteinModelPortal	P80572.
SMR	P80572. Positions 5-376.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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.
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_PEA

Accession

Primary (citable) accession number: P80572

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	December 14, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program