Reviewed, UniProtKB/Swiss-Prot P81600 (ADHH_GADMO)

Names and origin

Protein names	Recommended name:     Alcohol dehydrogenase class-3 chain H     EC=1.1.1.1 Alternative name(s):     Alcohol dehydrogenase class-III chain H     S-(hydroxymethyl)glutathione dehydrogenase     EC=1.1.1.284     Glutathione-dependent formaldehyde dehydrogenase       Short name=GSH-FDH       Short name=FALDH       Short name=FDH     EC=1.1.1.-
Organism	Gadus morhua (Atlantic cod)
Taxonomic identifier	8049 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Paracanthopterygii › Gadiformes › Gadidae › Gadus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subunit structure	Homodimer or heterodimer with L chain.
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
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 zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Alcohol dehydrogenase class-3 chain H		PRO_0000160763
Sites
	Metal binding	46	1	Zinc 1; catalytic
	Metal binding	68	1	Zinc 1; catalytic
	Metal binding	98	1	Zinc 2
	Metal binding	101	1	Zinc 2
	Metal binding	104	1	Zinc 2
	Metal binding	112	1	Zinc 2
	Metal binding	175	1	Zinc 1; catalytic
	Site	116	1	Important for FDH activity and activation by fatty acids By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylalanine Ref.1 Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P81600-1 [UniParc]. Last modified July 15, 1999. Version 1. Checksum: 0B9760AB77329FE3	FASTA	375	39,669
	10 20 30 40 50 60 ATAGQVIKCK AAVAWEAGKP LSLEEVEVAP PRAGEVRIKV VATGVCHTDA YTLSGSDPEG 70 80 90 100 110 120 AFPVILGHEG AGLVESVGEG VTKFKAGDTV IPLYVPQCGE CKFCKNPKTN LCQKIRVTQG 130 140 150 160 170 180 RGLMPDNTSR FTCKGKQLFH FMGTSTFSEY TVVADISLAN VDPKAPLDKV CLLGCGISTG 190 200 210 220 230 240 YGAALNTAKV EPGSTCAVFG LGAVGLAAIM GCKVAGATRI IGVDINPEKF GKAAEFGATE 250 260 270 280 290 300 CLNPKDHARP VQEVLVEMTD GGVDYSFECI GNVEIMRSAL EACHKGWGES VIIGVAGAGQ 310 320 330 340 350 360 EIATRPFQLV TGRVWKATAF GGWKSVESVP KLVEDYMNKK LKVDEFVTHT LPFDSINEGF 370 DLMHAGKSIR CVLTF

References

[1]

"Isozyme multiplicity with anomalous dimer patterns in a class III alcohol dehydrogenase. Effects on the activity and quaternary structure of residue exchanges at 'non-functional' sites in a native protein." Danielsson O., Shafqat J., Estonius M., El-Ahmad M., Joernvall H. Biochemistry 35:14561-14568(1996) [PubMed: 8931553] [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.

Cross-references

3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
SMR	P81600. Positions 3-373.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P81600.
Enzyme and pathway databases
BRENDA	1.1.1.1. 39336. 1.1.1.284. 39336.
Family and domain databases
InterPro	IPR014183. ADH_3. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR02818. adh_III_F_hyde. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADHH_GADMO

Accession

Primary (citable) accession number: P81600

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 15, 1999
Last modified:	September 22, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)