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Q51669 (GFA_PARDE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione-dependent formaldehyde-activating enzyme

EC=4.4.1.22
Alternative name(s):
S-(hydroxymethyl)glutathione synthase
Gene names
Name:gfa
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione. Ref.2

Catalytic activity

S-(hydroxymethyl)glutathione = glutathione + formaldehyde. HAMAP-Rule MF_00723

Cofactor

Binds 2 zinc ions per subunit.

Pathway

One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (glutathione route): step 1/3. HAMAP-Rule MF_00723

Subunit structure

Homodimer.

Sequence similarities

Belongs to the Gfa family.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processformaldehyde catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionS-(hydroxymethyl)glutathione synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 194193Glutathione-dependent formaldehyde-activating enzyme HAMAP-Rule MF_00723
PRO_0000220321

Sites

Metal binding311Zinc 1; structural
Metal binding331Zinc 1; structural
Metal binding521Zinc 2; catalytic
Metal binding541Zinc 2; catalytic
Metal binding571Zinc 2; catalytic
Metal binding991Zinc 1; structural
Metal binding1021Zinc 1; structural

Secondary structure

......................................... 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q51669 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 95B6E386B1756619

FASTA19420,967
        10         20         30         40         50         60 
MVDTSGVKIH PAVDNGIKPA QPGFAGGTLH CKCSTNPVRV AVRAQTAHNH VCGCTKCWKP 

        70         80         90        100        110        120 
EGAIFSQVAV VGRDALEVLE GAEKLEIVNA EAPIQRHRCR DCGVHMYGRI ENRDHPFYGL 

       130        140        150        160        170        180 
DFVHTELSDE DGWSAPEFAA FVSSIIESGV DPSRMEAIRA RLRELGLEPY DALSPPLMDA 

       190 
IATHIAKRSG ALAA 

« Hide

References

[1]"S-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?"
Harms N., Ras J., Reijnders W.N.M., van Spanning R.J.M., Stouthamer A.H.
J. Bacteriol. 178:6296-6299(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy."
Goenrich M., Bartoschek S., Hagemeier C.H., Griesinger C., Vorholt J.A.
J. Biol. Chem. 277:3069-3072(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16, FUNCTION.
[3]"A dynamic zinc redox switch."
Neculai A.M., Neculai D., Griesinger C., Vorholt J.A., Becker S.
J. Biol. Chem. 280:2826-2830(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U34346 Genomic DNA. Translation: AAC44550.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X6MX-ray2.35A/B/C/D1-194[»]
1XA8X-ray2.40A/B/C/D1-194[»]
ProteinModelPortalQ51669.
SMRQ51669. Positions 1-194.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00562; UER00621.

Family and domain databases

Gene3D3.90.1590.10. 1 hit.
HAMAPMF_00723. Formald_GSH.
InterProIPR014185. Formald_GSH.
IPR006913. GFA/CENP-V.
IPR011057. Mss4-like.
[Graphical view]
PfamPF04828. GFA. 1 hit.
[Graphical view]
PIRSFPIRSF033318. Formald_GSH. 1 hit.
SUPFAMSSF51316. SSF51316. 1 hit.
TIGRFAMsTIGR02820. formald_GSH. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ51669.

Entry information

Entry nameGFA_PARDE
AccessionPrimary (citable) accession number: Q51669
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 68 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

PATHWAY comments

Index of metabolic and biosynthesis pathways