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Q51669

- GFA_PARDE

UniProt

Q51669 - GFA_PARDE

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Protein
Glutathione-dependent formaldehyde-activating enzyme
Gene
gfa
Organism
Paracoccus denitrificans
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione.1 Publication

Catalytic activityi

S-(hydroxymethyl)glutathione = glutathione + formaldehyde.UniRule annotation

Cofactori

Binds 2 zinc ions per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311Zinc 1; structural
Metal bindingi33 – 331Zinc 1; structural
Metal bindingi52 – 521Zinc 2; catalytic
Metal bindingi54 – 541Zinc 2; catalytic
Metal bindingi57 – 571Zinc 2; catalytic
Metal bindingi99 – 991Zinc 1; structural
Metal bindingi102 – 1021Zinc 1; structural

GO - Molecular functioni

  1. S-(hydroxymethyl)glutathione synthase activity Source: UniProtKB-HAMAP
  2. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. formaldehyde catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00562; UER00621.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione-dependent formaldehyde-activating enzyme (EC:4.4.1.22)
Alternative name(s):
S-(hydroxymethyl)glutathione synthase
Gene namesi
Name:gfa
OrganismiParacoccus denitrificans
Taxonomic identifieri266 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 194193Glutathione-dependent formaldehyde-activating enzymeUniRule annotation
PRO_0000220321Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144
Beta strandi27 – 304
Beta strandi34 – 363
Beta strandi39 – 424
Beta strandi47 – 526
Beta strandi55 – 573
Beta strandi64 – 729
Helixi73 – 753
Beta strandi76 – 805
Helixi82 – 843
Beta strandi85 – 884
Beta strandi92 – 998
Turni100 – 1023
Beta strandi105 – 1106
Turni116 – 1194
Beta strandi120 – 1234
Helixi125 – 1273
Beta strandi138 – 1414
Helixi142 – 1487
Helixi152 – 1543
Helixi155 – 16410
Beta strandi171 – 1733
Helixi175 – 18915
Beta strandi190 – 1923

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X6MX-ray2.35A/B/C/D2-194[»]
1XA8X-ray2.40A/B/C/D2-194[»]
ProteinModelPortaliQ51669.
SMRiQ51669. Positions 1-194.

Miscellaneous databases

EvolutionaryTraceiQ51669.

Family & Domainsi

Sequence similaritiesi

Belongs to the Gfa family.

Family and domain databases

Gene3Di3.90.1590.10. 1 hit.
HAMAPiMF_00723. Formald_GSH.
InterProiIPR014185. Formald_GSH.
IPR006913. GFA/CENP-V.
IPR011057. Mss4-like.
[Graphical view]
PfamiPF04828. GFA. 1 hit.
[Graphical view]
PIRSFiPIRSF033318. Formald_GSH. 1 hit.
SUPFAMiSSF51316. SSF51316. 1 hit.
TIGRFAMsiTIGR02820. formald_GSH. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q51669-1 [UniParc]FASTAAdd to Basket

« Hide

MVDTSGVKIH PAVDNGIKPA QPGFAGGTLH CKCSTNPVRV AVRAQTAHNH    50
VCGCTKCWKP EGAIFSQVAV VGRDALEVLE GAEKLEIVNA EAPIQRHRCR 100
DCGVHMYGRI ENRDHPFYGL DFVHTELSDE DGWSAPEFAA FVSSIIESGV 150
DPSRMEAIRA RLRELGLEPY DALSPPLMDA IATHIAKRSG ALAA 194
Length:194
Mass (Da):20,967
Last modified:January 23, 2007 - v3
Checksum:i95B6E386B1756619
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34346 Genomic DNA. Translation: AAC44550.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34346 Genomic DNA. Translation: AAC44550.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X6M X-ray 2.35 A/B/C/D 2-194 [» ]
1XA8 X-ray 2.40 A/B/C/D 2-194 [» ]
ProteinModelPortali Q51669.
SMRi Q51669. Positions 1-194.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00562 ; UER00621 .

Miscellaneous databases

EvolutionaryTracei Q51669.

Family and domain databases

Gene3Di 3.90.1590.10. 1 hit.
HAMAPi MF_00723. Formald_GSH.
InterProi IPR014185. Formald_GSH.
IPR006913. GFA/CENP-V.
IPR011057. Mss4-like.
[Graphical view ]
Pfami PF04828. GFA. 1 hit.
[Graphical view ]
PIRSFi PIRSF033318. Formald_GSH. 1 hit.
SUPFAMi SSF51316. SSF51316. 1 hit.
TIGRFAMsi TIGR02820. formald_GSH. 1 hit.
ProtoNeti Search...

Publicationsi

  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. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.

Entry informationi

Entry nameiGFA_PARDE
AccessioniPrimary (citable) accession number: Q51669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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