EC 1.1.1.284
Glutathione-dependent formaldehyde dehydrogenase
GSH-FDH
FALDH
FDH
EC 1.1.1.-
Alcohol dehydrogenase class-3
EC 1.1.1.1
Alcohol dehydrogenase class-III

Gene name

	Name:	frmA
	Synonyms:	adhC
	OrderedLocusNames:	b0356, JW0347

From

Escherichia coli (strain K12)

[TaxID: 83333]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; Nashimoto H., Saito N.; Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Ito K., Matsumoto K., Tsuru D., Yoshimoto T.; Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[6]	PROTEIN SEQUENCE OF 1-47, FUNCTION, COFACTOR, AND SUBUNIT. DOI=10.1021/bi00117a025; PubMed=1731906 [NCBI, ExPASy, EBI, Israel, Japan] Gutheil W.G., Holmquist B., Vallee B.L.; "Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase."; Biochemistry 31:475-481(1992).
[7]	INDUCTION. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1128/JB.186.20.6714-6720.2004; PubMed=15466022 [NCBI, ExPASy, EBI, Israel, Japan] Herring C.D., Blattner F.R.; "Global transcriptional effects of a suppressor tRNA and the inactivation of the regulator frmR."; J. Bacteriol. 186:6714-6720(2004).

Comments

FUNCTION: Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates.
CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)⁺ = S-formylglutathione + NAD(P)H.
CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: Induced by formaldehyde and repressed by frmR.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
SEQUENCE CAUTION:
- Sequence=AAB18081.1; Type=Frameshift; Positions=26;
- Sequence=BAA12834.1; Type=Frameshift; Positions=26;

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

D85613; BAA12834.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D38504; BAA22412.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U73857; AAB18081.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73459.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76138.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D64763; D64763.

RefSeq

AP_001008.1; -.
NP_414890.1; -.

3D structure databases

HSSP

P11766; 1M6H. [HSSP ENTRY / PDB]

ModBase

P25437.

Protein-protein interaction databases

DIP

DIP:2901N; -.

IntAct

P25437; -.

Enzyme and pathway databases

BioCyc

EcoCyc:ADHC-MON; -.
MetaCyc:ADHC-MON; -.

Organism-specific databases

EchoBASE

EB4303; -.

EcoGene

EG50010; frmA.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
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

P25437.

Genome annotation databases

GeneID

944988; -.

GenomeReviews

U00096_GR; b0356.
AP009048_GR; JW0347.

KEGG

ecj:JW0347; -.
eco:b0356; -.

Phylogenomic databases

HOGENOM

P25437; -.

Genome annotation databases

CMR

P25437; b0356.

Other

UniRef

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

Keywords

Complete proteome; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 369`	`369`	`S-(hydroxymethyl)glutathione dehydrogenase.`	`PRO_0000160775`
`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`	`169 169`		`Zinc 1; catalytic (By similarity).`
`CONFLICT`	`41 41`		`H -> E (in Ref. 6; AA sequence).`
`CONFLICT`	`46 46`		`T -> G (in Ref. 6; AA sequence).`

Sequence information

Length: 369 AA [This is the length of the unprocessed precursor]

Molecular weight: 39359 Da [This is the MW of the unprocessed precursor]

CRC64: 35B59078F8173521 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKSRAAVAFA PGKPLEIVEI DVAPPKKGEV LIKVTHTGVC HTDAFTLSGD DPEGVFPVVL 

        70         80         90        100        110        120 
GHEGAGVVVE VGEGVTSVKP GDHVIPLYTA ECGECEFCRS GKTNLCVAVR ETQGKGLMPD 

       130        140        150        160        170        180 
GTTRFSYNGQ PLYHYMGCST FSEYTVVAEV SLAKINPEAN HEHVCLLGCG VTTGIGAVHN 

       190        200        210        220        230        240 
TAKVQPGDSV AVFGLGAIGL AVVQGARQAK AGRIIAIDTN PKKFDLARRF GATDCINPND 

       250        260        270        280        290        300 
YDKPIKDVLL DINKWGIDHT FECIGNVNVM RAALESAHRG WGQSVIIGVA VAGQEISTRP 

       310        320        330        340        350        360 
FQLVTGRVWK GSAFGGVKGR SQLPGMVEDA MKGDIDLEPF VTHTMSLDEI NDAFDLMHEG 


KSIRTVIRY

P25437 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