[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=C-83; PubMed=8169197 [NCBI, ExPASy, EBI, Israel, Japan] Ito K., Takahashi M., Yoshimoto T., Tsuru D.; "Cloning and high-level expression of the glutathione-independent formaldehyde dehydrogenase gene from Pseudomonas putida."; J. Bacteriol. 176:2483-2491(1994).
[2]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). DOI=10.1016/S0022-2836(02)01066-5; PubMed=12445786 [NCBI, ExPASy, EBI, Israel, Japan] Tanaka N., Kusakabe Y., Ito K., Yoshimoto T., Nakamura K.T.; "Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases."; J. Mol. Biol. 324:519-533(2002).

Comments

FUNCTION: Catalyzes the oxidation of long-chain alcohols but is inactive against ethanol.
CATALYTIC ACTIVITY: Formaldehyde + NAD⁺ + H₂O = formate + NADH.
CATALYTIC ACTIVITY: An alcohol + NAD⁺ = an aldehyde or ketone + NADH.
COFACTOR: Binds 2 zinc ions per subunit.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:   K_M=0.25 mM for formaldehyde;
pH dependence:   Optimum pH is 8.9. Active from pH 5 to 10;
Temperature dependence:   Thermostable up to 60 degrees Celsius;
SUBUNIT: Homotetramer.
SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.

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

D21201; BAA04743.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A55577; A55577.

3D structure databases

PDB

1KOL; X-ray; 1.65 A; A/B=1-399.

[ExPASy / RCSB / EBI]

PDBsum

1KOL; -.

ModBase

P46154.

Ontologies

GO:0018467;	Molecular function: formaldehyde dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
IPR014184; HCHO_DHase_non_GSH.
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

TIGR02819; fdhA_non_GSH; 1.

PROSITE

PS00059; ADH_ZINC; 1.

Other

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

Keywords

3D-structure; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 399`	`398`	`Glutathione-independent formaldehyde dehydrogenase.`	`PRO_0000160757`
`REGION`	`172 338`	`167`	`Cofactor-binding.`
`METAL`	`47 47`		`Zinc 1 (catalytic).`
`METAL`	`68 68`		`Zinc 1 (catalytic).`
`METAL`	`98 98`		`Zinc 2.`
`METAL`	`101 101`		`Zinc 2.`
`METAL`	`104 104`		`Zinc 2.`
`METAL`	`112 112`		`Zinc 2.`
`METAL`	`177 177`		`Zinc 1 (catalytic).`
`STRAND`	`4 11`	`8`
`STRAND`	`14 20`	`7`
`STRAND`	`37 45`	`9`
`HELIX`	`48 54`	`7`
`STRAND`	`70 77`	`8`
`STRAND`	`89 91`	`3`
`STRAND`	`94 96`	`3`
`STRAND`	`99 101`	`3`
`HELIX`	`102 105`	`4`
`HELIX`	`109 111`	`3`
`STRAND`	`113 115`	`3`
`STRAND`	`117 120`	`4`
`STRAND`	`122 124`	`3`
`STRAND`	`136 144`	`9`
`HELIX`	`145 148`	`4`
`HELIX`	`155 160`	`6`
`HELIX`	`162 165`	`4`
`HELIX`	`166 169`	`4`
`HELIX`	`171 181`	`11`
`STRAND`	`189 193`	`5`
`HELIX`	`197 208`	`12`
`STRAND`	`212 219`	`8`
`HELIX`	`221 229`	`9`
`STRAND`	`233 236`	`4`
`STRAND`	`239 241`	`3`
`HELIX`	`243 251`	`9`
`STRAND`	`252 254`	`3`
`STRAND`	`256 261`	`6`
`HELIX`	`274 276`	`3`
`HELIX`	`282 290`	`9`
`STRAND`	`296 299`	`4`
`HELIX`	`313 316`	`4`
`STRAND`	`320 322`	`3`
`HELIX`	`324 329`	`6`
`STRAND`	`333 338`	`6`
`HELIX`	`341 353`	`13`
`HELIX`	`359 363`	`5`
`STRAND`	`365 368`	`4`
`HELIX`	`370 372`	`3`
`HELIX`	`373 382`	`10`
`STRAND`	`387 390`	`4`

Sequence information

Length: 399 AA [This is the length of the unprocessed precursor]

Molecular weight: 42082 Da [This is the MW of the unprocessed precursor]

CRC64: EBBA418C97E76A9F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGNRGVVYL GSGKVEVQKI DYPKMQDPRG KKIEHGVILK VVSTNICGSD QHMVRGRTTA 

        70         80         90        100        110        120 
QVGLVLGHEI TGEVIEKGRD VENLQIGDLV SVPFNVACGR CRSCKEMHTG VCLTVNPARA 

       130        140        150        160        170        180 
GGAYGYVDMG DWTGGQAEYL LVPYADFNLL KLPDRDKAME KIRDLTCLSD ILPTGYHGAV 

       190        200        210        220        230        240 
TAGVGPGSTV YVAGAGPVGL AAAASARLLG AAVVIVGDLN PARLAHAKAQ GFEIADLSLD 

       250        260        270        280        290        300 
TPLHEQIAAL LGEPEVDCAV DAVGFEARGH GHEGAKHEAP ATVLNSLMQV TRVAGKIGIP 

       310        320        330        340        350        360 
GLYVTEDPGA VDAAAKIGSL SIRFGLGWAK SHSFHTGQTP VMKYNRALMQ AIMWDRINIA 

       370        380        390 
EVVGVQVISL DDAPRGYGEF DAGVPKKFVI DPHKTFSAA

P46154 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