P81601 (ADHL_GADMO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Alcohol dehydrogenase class-3 chain L EC=1.1.1.1 Alternative name(s): Alcohol dehydrogenase class-III chain L 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	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.
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 H 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
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 – 375	375	Alcohol dehydrogenase class-3 chain L		PRO_0000160764
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)
	P81601 [UniParc]. Last modified July 15, 1999. Version 1. Checksum: AEFE01C99243DBC9	FASTA	375	39,703
	10 20 30 40 50 60 ATVGKTIRCR AAVAWEAGKP LSMEEVEVAP PQAGEVRIKI VATGICHTDA YTLSGSDPEG 70 80 90 100 110 120 VFPSVLGHEG AGIVESVGEG VTKFKSGDAV IPLYVPQCGE CKFCKNPKTN LCQKIRLTQG 130 140 150 160 170 180 KGLMPNGTSR FSCNGQVLFH FMGSSTFSEY TVVAEISLAK VHEKAPLDKV CLLGCAISTG 190 200 210 220 230 240 YGAALNTAKV EAGSTCAVFG LGALGLAVIM GCQAAGASRI IAIDVNPDKF RIAKEFGATD 250 260 270 280 290 300 LVNPKDHSKP VEQVLVEMTD GGVDYSFECV GNIAVMRAAL EACHKGWGTS VIIGVAAAGQ 310 320 330 340 350 360 EISTRPFQLV TGRTWKGTAF GGYKSVESVP KLVEEYMNKK VKVDEFVTHT LPFEKIHEGF 370 DLMGAGKSIR TVLNY

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.
+	Additional computationally mapped references.

Cross-references

3D structure databases
ProteinModelPortal	P81601.
SMR	P81601. Positions 5-373.
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

ADHL_GADMO

Accession

Primary (citable) accession number: P81601

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 15, 1999
Last modified:	December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program