Reviewed, UniProtKB/Swiss-Prot Q17335 (ADHX_CAEEL)

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.-

Gene names

ORF Names:

H24K24.3

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	384 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.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
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 Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	S-(hydroxymethyl)glutathione dehydrogenase activity Ref.1 Non-traceable author statement. Source: UniProtKB alcohol dehydrogenase activity, zinc-dependent Ref.1 Non-traceable author statement. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform a (identifier: Q17335-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform b (identifier: Q17335-2)

The sequence of this isoform differs from the canonical sequence as follows:
     41-41: K → KFQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 384	384	Alcohol dehydrogenase class-3		PRO_0000160770
Sites
	Metal binding	48	1	Zinc 1; catalytic By similarity
	Metal binding	70	1	Zinc 1; catalytic By similarity
	Metal binding	100	1	Zinc 2 By similarity
	Metal binding	103	1	Zinc 2 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	114	1	Zinc 2 By similarity
	Metal binding	177	1	Zinc 1; catalytic By similarity
Natural variations
	Alternative sequence	41	1	K → KFQ in isoform b.		VSP_000208

Sequences

	Sequence		Length	Mass (Da)
	Isoform a [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E7FA7F7D55CD3908	FASTA	384	41,292
	10 20 30 40 50 60 MSSTAGQVIN CKAAVAWSAK APLSIETIQV APPKAHEVRV KILYTAVCHT DAYTLDGHDP 70 80 90 100 110 120 EGLFPVVLGH EGSGIVESVG EGVTGFAPGD HVVPLYVPQC KECEYCKNPK TNLCQKIRIS 130 140 150 160 170 180 QGNGFMPDGS SRFTCNGKQL FHFMGCSTFS EYTVVADISL CKVNPEAPLE KVSLLGCGIS 190 200 210 220 230 240 TGYGAVLNTC KVEEGSTVAV WGLGAVGLAV IMGAKAAGAK KIVGIDLIES KFESAKFFGA 250 260 270 280 290 300 TECINPKSVE LPEGKSFQAW LVEQFDGGFD YTFECIGNVH TMRQALEAAH KGWGVSCIIG 310 320 330 340 350 360 VAGAGQEIAT RPFQLVTGRT WKGTAFGGWK SVESVPRLVD DYMNKKLLID EFITHRWNID 370 380 DINTAFDVLH KGESLRSVLA FEKI
	Isoform b. Checksum: B27E1DF5ADF4EA5D	FASTA	386	41,568
	10 20 30 40 50 60 MSSTAGQVIN CKAAVAWSAK APLSIETIQV APPKAHEVRV KFQILYTAVC HTDAYTLDGH 70 80 90 100 110 120 DPEGLFPVVL GHEGSGIVES VGEGVTGFAP GDHVVPLYVP QCKECEYCKN PKTNLCQKIR 130 140 150 160 170 180 ISQGNGFMPD GSSRFTCNGK QLFHFMGCST FSEYTVVADI SLCKVNPEAP LEKVSLLGCG 190 200 210 220 230 240 ISTGYGAVLN TCKVEEGSTV AVWGLGAVGL AVIMGAKAAG AKKIVGIDLI ESKFESAKFF 250 260 270 280 290 300 GATECINPKS VELPEGKSFQ AWLVEQFDGG FDYTFECIGN VHTMRQALEA AHKGWGVSCI 310 320 330 340 350 360 IGVAGAGQEI ATRPFQLVTG RTWKGTAFGG WKSVESVPRL VDDYMNKKLL IDEFITHRWN 370 380 IDDINTAFDV LHKGESLRSV LAFEKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Caenorhabditis elegans contains genes encoding two new members of the Zn-containing alcohol dehydrogenase family." Glasner J.D., Kocher T.D., Collins J.J. J. Mol. Evol. 41:46-53(1995) [PubMed: 7608988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U18781 mRNA. Translation: AAB03374.1. AC006663 Genomic DNA. Translation: AAF39899.1. AC006663 Genomic DNA. Translation: AAL32231.1.
RefSeq	NP_001024016.1. NP_741507.1.
UniGene	Cel.17999
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
ModBase	Search...
Protein-protein interaction databases
STRING	Q17335.
Proteomic databases
PRIDE	Q17335.
Genome annotation databases
Ensembl	H24K24.3a.1; H24K24.3a.1; H24K24.3; Caenorhabditis elegans. [Genome view] H24K24.3a.2; H24K24.3a.2; H24K24.3; Caenorhabditis elegans. [Genome view] H24K24.3b; H24K24.3b; H24K24.3; Caenorhabditis elegans. [Genome view]
GeneID	178597.
KEGG	cel:H24K24.3.
UCSC	H24K24.3a.1. c. elegans.
Organism-specific databases
CTD	178597.
WormBase	WBGene00019240. H24K24.3.
WormPep	H24K24.3a. CE23822. [WorfDB] H24K24.3b. CE29978. [WorfDB]
Phylogenomic databases
OMA	KSFQAWL.
Enzyme and pathway databases
BRENDA	1.1.1.1. 672. 1.1.1.284. 672.
Gene expression databases
ArrayExpress	Q17335.
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...
Other Resources
NextBio	901794.

Entry information

Entry name

ADHX_CAEEL

Accession

Primary (citable) accession number: Q17335
Secondary accession number(s): Q8WSP4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project