Reviewed, UniProtKB/Swiss-Prot P80467 (ADHX_UROHA)

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	Uromastyx hardwickii (Indian spiny-tailed lizard)
Taxonomic identifier	40250 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Iguania › Acrodonta › Agamidae › Uromastycinae › Saara

Protein attributes

Sequence length	373 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.
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 – 373	373	Alcohol dehydrogenase class-3		PRO_0000160767
Sites
	Metal binding	44	1	Zinc 1; catalytic
	Metal binding	66	1	Zinc 1; catalytic
	Metal binding	96	1	Zinc 2
	Metal binding	99	1	Zinc 2
	Metal binding	102	1	Zinc 2
	Metal binding	110	1	Zinc 2
	Metal binding	173	1	Zinc 1; catalytic
	Site	114	1	Important for FDH activity and activation by fatty acids By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylalanine Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P80467-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 2BB3B44A0A9FCF06	FASTA	373	39,430
	10 20 30 40 50 60 ASGVIKCKAA VAWEAGKPLS IEEIEVAPPK AHEVRVKIIA TAVCHTDAYT LSGADPEGSF 70 80 90 100 110 120 PVILGHEGAG IVESVGEGVT KFKPGDTVIP LYIPQCGECK FCLNPKTNLC QKIRVTQGKG 130 140 150 160 170 180 VMPDGTSRFT CKGKQVLHFM GTSTFSEYTV VADISLTKIN ASAPLDKVCL LGCGVSTGYG 190 200 210 220 230 240 AALNTAKVEP GSTCAVFGLG GVGLAVIMGC KVAGASRIIG IDLNKDKFAK AKEFGATECI 250 260 270 280 290 300 SPADFKKPIQ EVLIEMTDGG VDYSFECIGN VGVMRAALEA CHKGWGVSVI VGVAAAGQEI 310 320 330 340 350 360 ATRPFQLVTG RTWKGTAFGG WKSVESVPKL VDEYMSKKMK VDEFVTHTLP FEQINEAFEL 370 MHAGKSIRSV LKF

References

[1]	"Alcohol dehydrogenase of class III: consistent patterns of structural and functional conservation in relation to class I and other proteins." Hjelmqvist L., Shafqat J., Siddiqi A.R., Joernvall H. FEBS Lett. 373:212-216(1995) [PubMed: 7589468] [Abstract] Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases
PIR	S68061.
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
SMR	P80467. Positions 1-372.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P80467.
Enzyme and pathway databases
BRENDA	1.1.1.1. 189323. 1.1.1.284. 189323.
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_UROHA

Accession

Primary (citable) accession number: P80467

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	October 13, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)