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Reviewed, UniProtKB/Swiss-Prot Q3Z550 (FRMA_SHISS)

Last modified June 16, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    S-(hydroxymethyl)glutathione dehydrogenase
    EC=1.1.1.284
Alternative name(s):
    Glutathione-dependent formaldehyde dehydrogenase
      Short name=GSH-FDH
      Short name=FALDH
      Short name=FDH
    EC=1.1.1.-
    Alcohol dehydrogenase class-3
    EC=1.1.1.1
    Alcohol dehydrogenase class-III
Gene names
Name: frmA
Ordered Locus Names: SSON_0335
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent By similarity.

Catalytic activity

S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369S-(hydroxymethyl)glutathione dehydrogenase
PRO_0000341292

Sites

Metal binding401Zinc 1; catalytic By similarity
Metal binding621Zinc 1; catalytic By similarity
Metal binding921Zinc 2 By similarity
Metal binding951Zinc 2 By similarity
Metal binding981Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1691Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3Z550-1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 37C601848801ECFB

FASTA36939,333
        10         20         30         40         50         60 
MKSRAAVAFA PGKPLEIVEI DVAPPKKGEV LIKVTHTGVC HTDAFTLSGD DPEGVFPVVL 

        70         80         90        100        110        120 
GHEGAGVVVE VGEGVTSVKP GDHVIPLYTA ECGECEFCRS GKTNLCVAVR ETQGKGLMPD 

       130        140        150        160        170        180 
GTTRFSYNGQ PLYHYMGCST FSEYTVVAEV SLAKINPEAN HEHVCLLGCG VTTGIGAVHN 

       190        200        210        220        230        240 
TAKVQPGDSV AVFGLGAIGL AVVQGARQAK AGRIIAIDTN PKKFDLARRF GATDCINPND 

       250        260        270        280        290        300 
YDKPIKDVLL DINKWGIDHT FECIGNVNVM RAALESAHRG WGQSVIIGVA GSGQEISTRP 

       310        320        330        340        350        360 
FQLVTGRVWK GSAFGGVKGR SQLPGMVEDA MKGDIDLEPF VTHTMSLDEI NDAFDLMHEG 


KSIRTVIRY 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000038 Genomic DNA. Translation: AAZ87112.1.
RefSeqYP_309347.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3668934.
GenomeReviewsGene locus SSON_0335 in contig CP000038_GR.
KEGGssn:SSON_0335.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3Z550.
OMAQ3Z550. AKFELAR.

Enzyme and pathway databases

BioCycSSON300269:SSO_0335-MON.

Family and domain databases

InterProIPR014183. ADH_3.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRMA_SHISS
AccessionPrimary (citable) accession number: Q3Z550
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: September 27, 2005
Last modified: June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents