UniProtKB - P46154 (FADH_PSEPU)
Protein
Glutathione-independent formaldehyde dehydrogenase
Gene
fdhA
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Functioni
Catalyzes the NAD+-dependent oxidation of formaldehyde and acetoaldehyde, and, to a lesser extent, long-chain alcohols, but is inactive against propionaldehyde, butyraldehyde, methanol and ethanol. Can also catalyze the dismutation of a wide range of aldehydes such as formaldehyde.2 Publications
Catalytic activityi
Cofactori
Zn2+Note: Binds 2 Zn2+ ions per subunit.
Activity regulationi
Inactivated by bipyridine and p-chloromercuribenzoate.1 Publication
Kineticsi
- KM=0.25 mM for formaldehyde
pH dependencei
Optimum pH is 8.9. Active from pH 5 to 10.
Temperature dependencei
Thermostable up to 60 degrees Celsius.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 47 | Zinc 1; catalytic | 1 | |
Metal bindingi | 68 | Zinc 1; catalytic | 1 | |
Metal bindingi | 98 | Zinc 2 | 1 | |
Metal bindingi | 101 | Zinc 2 | 1 | |
Metal bindingi | 104 | Zinc 2 | 1 | |
Metal bindingi | 112 | Zinc 2 | 1 | |
Metal bindingi | 177 | Zinc 1; catalytic | 1 |
GO - Molecular functioni
- formaldehyde dehydrogenase activity Source: UniProtKB-EC
- formaldehyde dismutase activity Source: UniProtKB-EC
- zinc ion binding Source: InterPro
Keywordsi
Molecular function | Oxidoreductase |
Ligand | Metal-binding, NAD, Zinc |
Enzyme and pathway databases
BRENDAi | 1.2.1.46, 5092 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:fdhA |
Organismi | Pseudomonas putida (Arthrobacter siderocapsulatus) |
Taxonomic identifieri | 303 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000160757 | 2 – 399 | Glutathione-independent formaldehyde dehydrogenaseAdd BLAST | 398 |
Interactioni
Subunit structurei
Homotetramer.
1 PublicationProtein-protein interaction databases
STRINGi | 1240350.AMZE01000028_gene1932 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P46154 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P46154 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 172 – 338 | Cofactor-bindingAdd BLAST | 167 |
Sequence similaritiesi
Belongs to the zinc-containing alcohol dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | COG1063, Bacteria |
Family and domain databases
InterProi | View protein in InterPro IPR013154, ADH_N IPR002328, ADH_Zn_CS IPR007698, AlaDH/PNT_NAD(H)-bd IPR011032, GroES-like_sf IPR014184, HCHO_DH_non_GSH IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF01262, AlaDh_PNT_C, 1 hit |
SUPFAMi | SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR02819, fdhA_non_GSH, 1 hit |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P46154-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSGNRGVVYL GSGKVEVQKI DYPKMQDPRG KKIEHGVILK VVSTNICGSD
60 70 80 90 100
QHMVRGRTTA QVGLVLGHEI TGEVIEKGRD VENLQIGDLV SVPFNVACGR
110 120 130 140 150
CRSCKEMHTG VCLTVNPARA GGAYGYVDMG DWTGGQAEYL LVPYADFNLL
160 170 180 190 200
KLPDRDKAME KIRDLTCLSD ILPTGYHGAV TAGVGPGSTV YVAGAGPVGL
210 220 230 240 250
AAAASARLLG AAVVIVGDLN PARLAHAKAQ GFEIADLSLD TPLHEQIAAL
260 270 280 290 300
LGEPEVDCAV DAVGFEARGH GHEGAKHEAP ATVLNSLMQV TRVAGKIGIP
310 320 330 340 350
GLYVTEDPGA VDAAAKIGSL SIRFGLGWAK SHSFHTGQTP VMKYNRALMQ
360 370 380 390
AIMWDRINIA EVVGVQVISL DDAPRGYGEF DAGVPKKFVI DPHKTFSAA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D21201 Genomic DNA Translation: BAA04743.1 |
PIRi | A55577 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D21201 Genomic DNA Translation: BAA04743.1 |
PIRi | A55577 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1KOL | X-ray | 1.65 | A/B | 2-399 | [»] | |
SMRi | P46154 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 1240350.AMZE01000028_gene1932 |
Chemistry databases
ChEMBLi | CHEMBL1293291 |
Phylogenomic databases
eggNOGi | COG1063, Bacteria |
Enzyme and pathway databases
BRENDAi | 1.2.1.46, 5092 |
Miscellaneous databases
EvolutionaryTracei | P46154 |
Family and domain databases
InterProi | View protein in InterPro IPR013154, ADH_N IPR002328, ADH_Zn_CS IPR007698, AlaDH/PNT_NAD(H)-bd IPR011032, GroES-like_sf IPR014184, HCHO_DH_non_GSH IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF08240, ADH_N, 1 hit PF01262, AlaDh_PNT_C, 1 hit |
SUPFAMi | SSF50129, SSF50129, 1 hit SSF51735, SSF51735, 1 hit |
TIGRFAMsi | TIGR02819, fdhA_non_GSH, 1 hit |
PROSITEi | View protein in PROSITE PS00059, ADH_ZINC, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FADH_PSEPU | |
Accessioni | P46154Primary (citable) accession number: P46154 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | January 23, 2007 | |
Last modified: | August 12, 2020 | |
This is version 120 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families