Reviewed, UniProtKB/Swiss-Prot A2XAZ3 (ADHX_ORYSI)

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:	ADHIII
ORF Names:	OsI_009236

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	381 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

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.
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
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 – 381	381	Alcohol dehydrogenase class-3		PRO_0000291457
Sites
	Metal binding	49	1	Zinc 1; catalytic By similarity
	Metal binding	71	1	Zinc 1; catalytic By similarity
	Metal binding	101	1	Zinc 2 By similarity
	Metal binding	104	1	Zinc 2 By similarity
	Metal binding	107	1	Zinc 2 By similarity
	Metal binding	115	1	Zinc 2 By similarity
	Metal binding	179	1	Zinc 1; catalytic By similarity
Experimental info
	Sequence conflict	48	1	L → F in AAB19117. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A2XAZ3-1 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: 5B8A11601EDB30CE	FASTA	381	40,795
	10 20 30 40 50 60 MASSTQGQVI TCKAAVAWEA NKPMTIEDVQ VAPPQAGEVR VKILFTALCH TDHYTWSGKD 70 80 90 100 110 120 PEGLFPCILG HEAAGIVESV GEGVTEVQPG DHVIPCYQAE CRECKFCKSG KTNLCGKVRA 130 140 150 160 170 180 ATGVGVMMND RKSRFSINGK PIYHFMGTST FSQYTVVHDV SVAKINPQAP LDKVCLLGCG 190 200 210 220 230 240 VSTGLGAVWN TAKVEAGSIV AIFGLGTVGL AVAEGAKSAG ASRIIGIDID SKKFDVAKNF 250 260 270 280 290 300 GVTEFVNPKD HDKPIQQVIV DLTDGGVDYS FECIGNVSVM RSALECCHKG WGTSVIVGVA 310 320 330 340 350 360 ASGQEISTRP FQLVTGRVWK GTAFGGFKSR SQVPWLVEKY LNKEIKVDEY VTHSMNLTDI 370 380 NKAFDLLHEG GCLRCVLATD K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the Arabidopsis and rice formaldehyde dehydrogenase genes: implications for the origin of plant ADH enzymes." Dolferus R., Osterman J.C., Peacock W.J., Dennis E.S. Genetics 146:1131-1141(1997) [PubMed: 9215914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. IR36.
[2]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U77637 Genomic DNA. Translation: AAB19117.1. CM000127 Genomic DNA. Translation: EAY88003.1.
PIR	T04164.
UniGene	Os.59290
3D structure databases
SMR	A2XAZ3. Positions 8-377.
ModBase	Search...
Organism-specific databases
Gramene	P93436.
Phylogenomic databases
HOGENOM	HBG753318.
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_ORYSI

Accession

Primary (citable) accession number: A2XAZ3
Secondary accession number(s): P93436, Q6K6C1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	March 20, 2007
Last modified:	February 9, 2010
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)