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P33160 (FDH_PSESR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Formate dehydrogenase

EC=1.2.1.2
Alternative name(s):
NAD-dependent formate dehydrogenase
Short name=FDH
OrganismPseudomonas sp. (strain 101) (Achromobacter parvulus T1)
Taxonomic identifier33067 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Formate + NAD+ = CO2 + NADH.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. FDH subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 401400Formate dehydrogenase
PRO_0000076027

Regions

Nucleotide binding202 – 2032NAD By similarity
Nucleotide binding283 – 2853NAD By similarity
Nucleotide binding333 – 3364NAD By similarity
Region2 – 147146Catalytic
Region148 – 334187Coenzyme-binding
Region335 – 40167Catalytic

Sites

Active site2851 By similarity
Active site3331Proton donor By similarity
Binding site3091NAD By similarity

Experimental info

Mutagenesis2561C → S or M: High resistance to inactivation by Hg(2+), Increased stability at 25 degree Celsius and decreased thermostability at 45 degree Celsius. Ref.4
Sequence conflict781D → S Ref.1
Sequence conflict139 – 1402TV → VT Ref.1
Sequence conflict1461C → V Ref.1
Sequence conflict216 – 2172VH → HV Ref.1
Sequence conflict3281N → D Ref.1

Secondary structure

........................................................................ 401
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33160 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 6B3EBA21F03A89A2

FASTA40144,136
        10         20         30         40         50         60 
MAKVLCVLYD DPVDGYPKTY ARDDLPKIDH YPGGQTLPTP KAIDFTPGQL LGSVSGELGL 

        70         80         90        100        110        120 
RKYLESNGHT LVVTSDKDGP DSVFERELVD ADVVISQPFW PAYLTPERIA KAKNLKLALT 

       130        140        150        160        170        180 
AGIGSDHVDL QSAIDRNVTV AEVTYCNSIS VAEHVVMMIL SLVRNYLPSH EWARKGGWNI 

       190        200        210        220        230        240 
ADCVSHAYDL EAMHVGTVAA GRIGLAVLRR LAPFDVHLHY TDRHRLPESV EKELNLTWHA 

       250        260        270        280        290        300 
TREDMYPVCD VVTLNCPLHP ETEHMINDET LKLFKRGAYI VNTARGKLCD RDAVARALES 

       310        320        330        340        350        360 
GRLAGYAGDV WFPQPAPKDH PWRTMPYNGM TPHISGTTLT AQARYAAGTR EILECFFEGR 

       370        380        390        400 
PIRDEYLIVQ GGALAGTGAH SYSKGNATGG SEEAAKFKKA V 

« Hide

References

[1]"NAD-dependent formate dehydrogenase of methylotrophic bacteria Pseudomonas sp. 101: cloning, expression, and study of the genetic structure."
Tishkov V.I., Galkin A.G., Egorov A.M.
Dokl. Akad. Nauk SSSR 317:745-748(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"NAD-dependent formate dehydrogenase from methylotrophic bacteria Pseudomonas sp. 101. I. Amino acid sequence."
Popov V.O., Shumilin I.A., Ustinnikova T.B., Lamzin V.S., Egorov T.A.
Bioorg. Khim. 16:324-335(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-394.
[3]"Crystal structure of NAD-dependent formate dehydrogenase."
Lamzin V.S., Aleshin A.E., Strokopytov B.V., Yukhnevich M.G., Popov V.O., Harutyunyan E.H., Wilson K.S.
Eur. J. Biochem. 206:441-452(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[4]"Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacements."
Tishkov V.I., Galkin A.G., Marchenko G.N., Egorova O.A., Sheluho D.V., Kulakova L.B., Dementieva L.A., Egorov A.M.
Biochem. Biophys. Res. Commun. 192:976-981(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-256.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRJU0334.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GO1X-ray2.10A1-401[»]
2GUGX-ray2.28A/B/C/D1-401[»]
2NACX-ray1.80A/B2-394[»]
2NADX-ray2.05A/B2-394[»]
ProteinModelPortalP33160.
SMRP33160. Positions 2-392.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.2. 5085.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33160.

Entry information

Entry nameFDH_PSESR
AccessionPrimary (citable) accession number: P33160
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references