S-(hydroxymethyl)glutathione dehydrogenase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P25437 (FRMA_ECOLI)

Last modified June 16, 2009. Version 84. History...

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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 names

Recommended 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
Synonyms:	adhC
Ordered Locus Names:	b0356, JW0347

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates. Ref.6
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. Ref.6
Subcellular location	Cytoplasm.
Induction	Induced by formaldehyde and repressed by frmR. Ref.7
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.
Sequence caution	The sequence AAB18081.1 differs from that shown. Reason: Frameshift at position 26. The sequence BAA12834.1 differs from that shown. Reason: Frameshift at position 26.

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Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ethanol oxidation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	S-(hydroxymethyl)glutathione dehydrogenase activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 369

369

S-(hydroxymethyl)glutathione dehydrogenase

PRO_0000160775

Sites

Metal binding

Zinc 1; catalytic By similarity

Metal binding

Zinc 1; catalytic By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

Zinc 2 By similarity

Metal binding

106

Zinc 2 By similarity

Metal binding

169

Zinc 1; catalytic By similarity

Experimental info

Sequence conflict

H → E AA sequence Ref.6

Sequence conflict

T → G AA sequence Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

P25437-1 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 35B59078F8173521
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FASTA

369

39,359

        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 VAGQEISTRP 

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


KSIRTVIRY

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Nashimoto H., Saito N. Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	Ito K., Matsumoto K., Tsuru D., Yoshimoto T. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase." Gutheil W.G., Holmquist B., Vallee B.L. Biochemistry 31:475-481(1992) [PubMed: 1731906] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-47, FUNCTION, COFACTOR, SUBUNIT.
[7]	"Global transcriptional effects of a suppressor tRNA and the inactivation of the regulator frmR." Herring C.D., Blattner F.R. J. Bacteriol. 186:6714-6720(2004) [PubMed: 15466022] [Abstract] Cited for: INDUCTION. Strain: K12 / MG1655 / ATCC 47076.

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Cross-references

Sequence databases
	D85613 Genomic DNA. Translation: BAA12834.1. Frameshift. D38504 Genomic DNA. Translation: BAA22412.1. U73857 Genomic DNA. Translation: AAB18081.1. Frameshift. U00096 Genomic DNA. Translation: AAC73459.1. AP009048 Genomic DNA. Translation: BAE76138.1.
PIR	D64763.
RefSeq	AP_001008.1. NP_414890.1.
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2901N.
IntAct	P25437. 5 interactions.
Genome annotation databases
GeneID	944988.
GenomeReviews	Gene locus JW0347 in contig AP009048_GR. Gene locus b0356 in contig U00096_GR.
KEGG	ecj:JW0347. eco:b0356.
Organism-specific databases
EchoBASE	EB4303.
EcoGene	EG50010. frmA.
CMR	Search...
Phylogenomic databases
HOGENOM	P25437.
OMA	P25437. AKFELAR.
Enzyme and pathway databases
BioCyc	EcoCyc:ADHC-MON. MetaCyc:ADHC-MON.
Family and domain databases
InterPro	IPR014183. ADH_3. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002328. ADH_Zn_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR02818. adh_III_F_hyde. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

FRMA_ECOLI

Accession

Primary (citable) accession number: P25437
Secondary accession number(s): P75696, Q2MC68, Q47533

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents