P80360 (ADHX_MYXGL) 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	Myxine glutinosa (Atlantic hagfish)
Taxonomic identifier	7769 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Hyperotreti › Myxiniformes › Myxinidae › Myxininae › Myxine

Protein attributes

Sequence length	376 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.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Liver and gut.
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 – 376	376	Alcohol dehydrogenase class-3		PRO_0000160765
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	176	1	Zinc 1; catalytic By similarity
	Site	117	1	Important for FDH activity and activation by fatty acids By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylserine Ref.1 Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P80360 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: FFD20C195FF67B5F	FASTA	376	39,747
	10 20 30 40 50 60 SKMDGQVIHC KAAVAWEAKK PLSLEEIEVA PPKAHEVRMK VLATAVCHTD AYTLSGVDPE 70 80 90 100 110 120 GSFPVVLGHE GAGIVESVGE GVTKFKPGDS VIPLYIPQCG ECKFCLNPKT NLCQKIRVTQ 130 140 150 160 170 180 GKGMMPDGTS RLTCRGKSLY HFMGASTFSE YAVVADISLC RVAPEAPPDR VCLLGCGVST 190 200 210 220 230 240 GYGAPLNTAK VEPGSTCAIF GLGAVGLAAI MGCRVAGASR IIAIDRNPDK FEKARIFGAT 250 260 270 280 290 300 DCVVPDASDK PISQVLGEMT DGGLDYTFEC VGNVGIMRAA LESCHKGWGV SVILGVAGGG 310 320 330 340 350 360 QEISTRPFQL VTGRTWKGAA FGGWKSVESV PKLVDDYMAG KIMVDEFVSH SLPFDSINEA 370 FDLMHAGKSI RTVLQL

References

[1]	"Alcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization." Danielsson O., Shafqat J., Estonius M., Joernvall H. Eur. J. Biochem. 225:1081-1088(1994) [PubMed: 7957198] [Abstract] Cited for: PROTEIN SEQUENCE, ACETYLATION AT SER-1. Tissue: Liver.
[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 SER-1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	S51187.
3D structure databases
ProteinModelPortal	P80360.
SMR	P80360. Positions 6-376.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG000195.
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_MYXGL

Accession

Primary (citable) accession number: P80360

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program