Reviewed, UniProtKB/Swiss-Prot Q1RFI7 (FRMA_ECOUT)

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
Ordered Locus Names:	UTI89_C0376

Organism

Escherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

364106 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ethanol oxidation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	S-(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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 369	369	S-(hydroxymethyl)glutathione dehydrogenase		PRO_0000341285
Sites
	Metal binding	40	1	Zinc 1; catalytic By similarity
	Metal binding	62	1	Zinc 1; catalytic By similarity
	Metal binding	92	1	Zinc 2 By similarity
	Metal binding	95	1	Zinc 2 By similarity
	Metal binding	98	1	Zinc 2 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	169	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1RFI7-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 760D615FF801ED20	FASTA	369	39,347
	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 PKKFELARRF 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

References

[1]

"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach." Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000243 Genomic DNA. Translation: ABE05877.1.
RefSeq	YP_539408.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RFI7.
Genome annotation databases
GeneID	3994398.
GenomeReviews	Gene locus UTI89_C0376 in contig CP000243_GR.
KEGG	eci:UTI89_C0376.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1RFI7.
OMA	AKFELAR.
Enzyme and pathway databases
BioCyc	ECOL364106:UTI89_C0376-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...

Entry information

Entry name

FRMA_ECOUT

Accession

Primary (citable) accession number: Q1RFI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	May 16, 2006
Last modified:	November 3, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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