Reviewed, UniProtKB/Swiss-Prot P79896 (ADHX_SPAAU)

Names and origin

Protein names	Recommended name:     Alcohol dehydrogenase class-3     EC=1.1.1.1 Alternative name(s):     Alcohol dehydrogenase class-III     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	Sparus aurata (Gilthead sea bream)
Taxonomic identifier	8175 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Perciformes › Percoidei › Sparidae › Sparus

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity.
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 By similarity.
Subcellular location	Cytoplasm Potential.
Tissue specificity	Expressed in the skeletal muscle, heart, gill filaments and liver, with highest levels in the kidney.
Developmental stage	Found in the eggs and in embryos 4, 8 and 12 hours after fertlization, as well as on all days post-hatching. Level of expression decreases during embryonal development but increases 4-fold from day 1 to day 21 after hatching.
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
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 – 376	376	Alcohol dehydrogenase class-3		PRO_0000160766
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

Sequences

	Sequence		Length	Mass (Da)
	P79896-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 306F27117F3F2313	FASTA	376	40,215
	10 20 30 40 50 60 METAGKVIKC KAAVAWEPGK PLSIEEVEVA PPNAHEVRIK LFATGVCHTD AYTLSGSDPE 70 80 90 100 110 120 GLFPVILGHE GAGTVESVGE GVTKFKPGDT VIPLYVPQCG ECKFCKNPKT NLCQKIRITQ 130 140 150 160 170 180 GQGLLPDKTS RFTCKGKQVF HFMGTSTFSE YTVVADISLA KVNEKAPMDK VCLLGCGIST 190 200 210 220 230 240 GYGAALNTAK VEPGSTCAVF GLGAVGLAVI MGCKVAGATR IIGIDLNPAK FETAKEFGAT 250 260 270 280 290 300 EFVNPKDHSK PIQEVLVEMT DGGVDYSFEC IGNVQIMRAA LEACHKGWGE SVIIGVAGAG 310 320 330 340 350 360 QEISTRPFQL VTGRVWKGTA FGGWKSVESV PKLVEDYMSK KLKVDEFVTH TLPFEKINEG 370 FELMHAGKSI RTVLTF

References

[1]	"Molecular cloning of fish alcohol dehydrogenase cDNA." Funkenstein B., Jakowlew S.B. Gene 174:159-164(1996) [PubMed: 8863743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Larva.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U84791 mRNA. Translation: AAB41888.1.
PIR	JC4967.
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
SMR	P79896. Positions 4-374.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P79896.
Enzyme and pathway databases
BRENDA	1.1.1.1. 191612. 1.1.1.284. 191612.
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

ADHX_SPAAU

Accession

Primary (citable) accession number: P79896

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 1, 1997
Last modified:	September 22, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)