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Reviewed, UniProtKB/Swiss-Prot B1LIP1 (FRMA_ECOSM)

Last modified February 9, 2010. Version 17. 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

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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: EcSMS35_0387
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processethanol oxidation

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionS-(hydroxymethyl)glutathione dehydrogenase activity

Inferred from electronic annotation. Source: EC

alcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369S-(hydroxymethyl)glutathione dehydrogenase
PRO_0000341284

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

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Sequences

Sequence LengthMass (Da)Tools
B1LIP1-1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 6614D0578802EDB0

FASTA36939,391
        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 
TAKVQPDDSV 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

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References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed: 18708504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000970 Genomic DNA. Translation: ACB18273.1.
RefSeqYP_001742490.1.

3D structure databases

SMRB1LIP1. Positions 1-368.
ModBaseSearch...

Genome annotation databases

GeneID6143543.
GenomeReviewsGene locus EcSMS35_0387 in contig CP000970_GR.
KEGGecm:EcSMS35_0387.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG753318.
OMAAKFELAR.

Family and domain databases

InterProIPR014183. ADH_3.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[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...

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Entry information

Entry nameFRMA_ECOSM
AccessionPrimary (citable) accession number: B1LIP1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: April 29, 2008
Last modified: February 9, 2010
This is version 17 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)

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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