P81431 (ADHX_OCTVU) 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	Octopus vulgaris (Common octopus)
Taxonomic identifier	6645 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Mollusca › Cephalopoda › Coleoidea › Neocoleoidea › Octopodiformes › Octopoda › Incirrata › Octopodidae › Octopus

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.
Subunit structure	Homodimer.
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_0000160768
Sites
	Metal binding	47	1	Zinc 1; catalytic
	Metal binding	69	1	Zinc 1; catalytic
	Metal binding	99	1	Zinc 2
	Metal binding	102	1	Zinc 2
	Metal binding	105	1	Zinc 2
	Metal binding	113	1	Zinc 2
	Metal binding	176	1	Zinc 1; catalytic
	Site	117	1	Important for FDH activity and activation by fatty acids By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylthreonine Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P81431 [UniParc]. Last modified December 15, 1998. Version 1. Checksum: B19CDA25C1261ACA	FASTA	378	40,400
	10 20 30 40 50 60 TDATGKPIKC MAAIAWEAKK PLSIEEVEVA PPKSGEVRIK ILHSGVCHTD AYTLEGIDPE 70 80 90 100 110 120 GIFPVILGHE GAGIVESIGE GVTSVKPGDT VIPLYVPQCY ECKFCLNPKT NLCQKIRVTQ 130 140 150 160 170 180 GKGVMPDGTT RFTCKGKEVF HFMGCSTFSE FTVVAEISIA KVNPKAALDK VCLLGCGIST 190 200 210 220 230 240 GYGAALNTAA VEKGSNCAVW GLGAVGLAVA MGCKAAGAAR IIGIDINESK FEIGKKFGIT 250 260 270 280 290 300 EFVNPKKFCK SVQKVLGEMT DVGVDFTFEC IGNVGVMRAA LESCHKGWGT SVIVGVAAHG 310 320 330 340 350 360 EEISTRPFQL VTGRVWKGTA FGGFKSRDSV PKLVDDYMNK KLLLDEFVSH KLSFKKINEA 370 FDLMHKGESI RAVLDIPE

References

[1]	"Origin of the human alcohol dehydrogenase system: implications from the structure and properties of the octopus protein." Kaiser R., Fernandez M.R., Pares X., Joernvall H. Proc. Natl. Acad. Sci. U.S.A. 90:11222-11226(1993) [PubMed: 8248232] [Abstract] Cited for: PROTEIN SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	A49662.
3D structure databases
ProteinModelPortal	P81431.
SMR	P81431. Positions 8-376.
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_OCTVU

Accession

Primary (citable) accession number: P81431

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	December 14, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)