Reviewed, UniProtKB/Swiss-Prot Q54TC2 (ADHX_DICDI)

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

Name:	adh5
ORF Names:	DDB_G0281865

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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
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 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 – 379	379	Alcohol dehydrogenase class-3		PRO_0000345023
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

Sequences

	Sequence		Length	Mass (Da)
	Q54TC2-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 5E5B438509D3E3C8	FASTA	379	40,553
	10 20 30 40 50 60 MSTEGKVITC KAAVAWEAKK PLVIEDIEVQ PPQKGEVRIK ILYTGVCHTD SYTLSGSDPE 70 80 90 100 110 120 GIFPCILGHE GGGIVESIGE GVTSVKVGDH VIPLYIPECG TCKFCTSNKT NLCSKIRITQ 130 140 150 160 170 180 GKGQMPDGTT RFKCKGKEIF HFMGTSTFSQ YTVLPEISCC VVREDAPLDK VCLLGCGITT 190 200 210 220 230 240 GFGAAKITAK VEEGSTVAIF GLGAVGLSVA QGAVDCGAKR IIGIDNNETK FGPGKDFGCT 250 260 270 280 290 300 EFINPSKDLP EGKTIQQHLV DITDGGVDYS FECIGNVNVM RAALECCHKG WGVSTIVGVA 310 320 330 340 350 360 PAGAEISTRP FQLVTGRVWK GSAFGGVKSR SQLPSIIDKY MDKKLKVDEY VTFTYPLNEI 370 NTAFDVMHEG KSLRSVVNL

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000043 Genomic DNA. Translation: EAL66492.1.
RefSeq	XP_640467.1.
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
SMR	Q54TC2. Positions 6-379.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54TC2.
Genome annotation databases
GeneID	8623280.
KEGG	ddi:DDB_0238276.
Organism-specific databases
dictyBase	DDB_G0281865. adh5.
Phylogenomic databases
eggNOG	KOG0022.
HOGENOM	HBG753318.
OMA	ALEATHK.
PhylomeDB	Q54TC2.
Family and domain databases
InterPro	IPR014183. ADH_3. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [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_DICDI

Accession

Primary (citable) accession number: Q54TC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)