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
	OrderedLocusNames:	EcSMS35_0387

From

Escherichia coli (strain SMS-3-5 / SECEC)

[TaxID: 439855]

[HAMAP proteome]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.; "Complete sequence of Escherichia coli SECEC SMS-3-5."; Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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

CP000970; ACB18273.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001742490.1; -.

3D structure databases

ModBase

B1LIP1.

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.

PROSITE

PS00059; ADH_ZINC; 1.

Genome annotation databases

GeneID

6143543; -.

GenomeReviews

CP000970_GR; EcSMS35_0387.

KEGG

ecm:EcSMS35_0387; -.

CMR

B1LIP1; EcSMS35_0387.

Other

ProtoNet

B1LIP1.

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`	`1 369`	`369`	`S-(hydroxymethyl)glutathione dehydrogenase.`	`PRO_0000341284`
`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).`

Sequence information

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

Molecular weight: 39391 Da [This is the MW of the unprocessed precursor]

CRC64: 6614D0578802EDB0 [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 
TAKVQPDDSV AVFGLGAIGL AVVQGARQAK AGRIIAIDTN PKKFDLARRF GATDCINPND 

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

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


KSIRTVIRY

B1LIP1 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