EC 1.1.1.1
Alcohol dehydrogenase class-III
S-(hydroxymethyl)glutathione dehydrogenase
EC 1.1.1.284
Glutathione-dependent formaldehyde dehydrogenase
GSH-FDH
FALDH
FDH
EC 1.1.1.-

Gene name

	Name:	adhI
	OrderedLocusNames:	RHOS4_11650
	ORFNames:	RSP_2576

From

Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)

[TaxID: 272943]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Rhodobacter.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8631716 [NCBI, ExPASy, EBI, Israel, Japan] Barber R.D., Rott M.A., Donohue T.J.; "Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides."; J. Bacteriol. 178:1386-1393(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.; "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Oxidizes long-chain aliphatic alcohols, long-chain hydroxylated fatty acids and S-hydroxymethylglutathione (hmGSH) in increasing order of preference. Shows little or no activity with short-chain aliphatic alcohols.
CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)⁺ = S-formylglutathione + NAD(P)H.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Homodimer (Probable).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L47326; AAB09774.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000143; ABA78733.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_352634.1; -.

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

P72324.

Enzyme and pathway databases

BioCyc

RSPH272943:RSP_2576-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004022;	Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0051903;	Molecular function: S-(hydroxymethyl)glutathione dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR014183; AlcDHase_3.
IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02818; adh_III_F_hyde; 1.

PROSITE

PS00059; ADH_ZINC; 1.

ProtoNet

P72324.

Genome annotation databases

GeneID

3720209; -.

GenomeReviews

CP000143_GR; RHOS4_11650.

KEGG

rsp:RSP_2576; -.

NMPDR

fig|272943.3.peg.1221; -.

Phylogenomic databases

HOGENOM

P72324; -.

Genome annotation databases

CMR

P72324; RHOS4_11650.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 376`	`376`	`Alcohol dehydrogenase class-3.`	`PRO_0000160780`
`METAL`	`40 40`		`Zinc 1; catalytic (By similarity).`
`METAL`	`62 62`		`Zinc 1; catalytic (By similarity).`
`METAL`	`92 92`		`Zinc 2 (By similarity).`
`METAL`	`95 95`		`Zinc 2 (By similarity).`
`METAL`	`98 98`		`Zinc 2 (By similarity).`
`METAL`	`106 106`		`Zinc 2 (By similarity).`
`METAL`	`170 170`		`Zinc 1; catalytic (By similarity).`

Sequence information

Length: 376 AA [This is the length of the unprocessed precursor]

Molecular weight: 39974 Da [This is the MW of the unprocessed precursor]

CRC64: 9144690996B32BB9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRTRAAVAVE AGKPLEIMEV NLEGPKAGEV MVEIKATGIC HTDEFTLSGA DPEGMFPAIL 

        70         80         90        100        110        120 
GHEGAGVVVE VGPGVTSVKP GDHVIPLYTP ECRQCPSCLS QKTNLCTAIR GTQGQGLMPD 

       130        140        150        160        170        180 
GTSRFSMLDG TPILHYMGCS TFSNYTVLPE IAVAKVRPDA PFDKICYIGC GVTTGIGAVI 

       190        200        210        220        230        240 
NTAKVEIGAK AVVFGLGGIG LNVIQGLKLA GADMIIGVDL NNAKKEWGER FGMTHFVNPS 

       250        260        270        280        290        300 
EIDGDVVAHL VNMTKTPFDQ IGGADYTFDC TGNVKVMRQA LEACHRGWGQ SIVIGVAPAG 

       310        320        330        340        350        360 
AEIQTRPFQL VTGRVWKGSA FGGARGRTDV PKIVDWYMEG KIQIDPMITH ILSLEEINKG 

       370 
FDLMHAGESI RSVVVF

P72324 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools