Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione-dependent formaldehyde-activating enzyme

Gene

gfa

Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score: -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.

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Pathwayi: formaldehyde degradation

This protein is involved in step 1 of the subpathway that synthesizes formate from formaldehyde (glutathione route).
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glutathione-dependent formaldehyde-activating enzyme (gfa)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway formaldehyde degradation, which is itself part of One-carbon metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes formate from formaldehyde (glutathione route), the pathway formaldehyde degradation and in One-carbon metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi31Zinc 1; structural1
Metal bindingi33Zinc 1; structural1
Metal bindingi52Zinc 2; catalytic1
Metal bindingi54Zinc 2; catalytic1
Metal bindingi57Zinc 2; catalytic1
Metal bindingi99Zinc 1; structural1
Metal bindingi102Zinc 1; structural1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayi
UPA00562;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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002203212 – 194Glutathione-dependent formaldehyde-activating enzymeAdd BLAST193

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ51669
SMRiQ51669
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51669

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 141GFASequence analysisAdd BLAST91

Sequence similaritiesi

Belongs to the Gfa family.Curated

Phylogenomic databases

eggNOGiENOG4108QBQ Bacteria
COG3791 LUCA

Family and domain databases

HAMAPiMF_00723 Formald_GSH, 1 hit
InterProiView protein in InterPro
IPR014185 Formald_GSH
IPR006913 GFA/CENP-V
IPR011057 Mss4-like_sf
PfamiView protein in Pfam
PF04828 GFA, 1 hit
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
        10         20         30         40         50
MVDTSGVKIH PAVDNGIKPA QPGFAGGTLH CKCSTNPVRV AVRAQTAHNH
60 70 80 90 100
VCGCTKCWKP EGAIFSQVAV VGRDALEVLE GAEKLEIVNA EAPIQRHRCR
110 120 130 140 150
DCGVHMYGRI ENRDHPFYGL DFVHTELSDE DGWSAPEFAA FVSSIIESGV
160 170 180 190
DPSRMEAIRA RLRELGLEPY DALSPPLMDA IATHIAKRSG ALAA
Length:194
Mass (Da):20,967
Last modified:January 23, 2007 - v3
Checksum:i95B6E386B1756619
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34346 Genomic DNA Translation: AAC44550.1
RefSeqiWP_011746365.1, NZ_PPGA01000008.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34346 Genomic DNA Translation: AAC44550.1
RefSeqiWP_011746365.1, NZ_PPGA01000008.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X6MX-ray2.35A/B/C/D2-194[»]
1XA8X-ray2.40A/B/C/D2-194[»]
ProteinModelPortaliQ51669
SMRiQ51669
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108QBQ Bacteria
COG3791 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00562;UER00621

Miscellaneous databases

EvolutionaryTraceiQ51669

Family and domain databases

HAMAPiMF_00723 Formald_GSH, 1 hit
InterProiView protein in InterPro
IPR014185 Formald_GSH
IPR006913 GFA/CENP-V
IPR011057 Mss4-like_sf
PfamiView protein in Pfam
PF04828 GFA, 1 hit
PIRSFiPIRSF033318 Formald_GSH, 1 hit
SUPFAMiSSF51316 SSF51316, 1 hit
TIGRFAMsiTIGR02820 formald_GSH, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiGFA_PARDE
AccessioniPrimary (citable) accession number: Q51669
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 88 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again