Reviewed, UniProtKB/Swiss-Prot P45382 (FADH_PARDE)

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.-

Gene names

Name:

flhA

Organism

Paracoccus denitrificans

Taxonomic identifier

266 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential for the oxidation of formaldehyde produced during methylotrophic growth.
Catalytic activity	S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Ontologies

Keywords
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	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
Molecular function	S-(hydroxymethyl)glutathione dehydrogenase 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 – 375	375	S-(hydroxymethyl)glutathione dehydrogenase		PRO_0000160779
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	170	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45382-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: D3A41572C1F26424	FASTA	375	39,919
	10 20 30 40 50 60 MRTRAAVALE AGKPLEVMEV NLEGPKAGEV MVEIKATGIC HTDEFTLSGA DPEGLFPSIL 70 80 90 100 110 120 GHEGAGVVVE VGPGVTSVKP GNHVIPLYTP ECRQCASCLS GKTNLCTAIR ATQGQGLMPD 130 140 150 160 170 180 GTSRFSMLDG TPIFHYMGCS TFSNYTVLPE IAVAKVREDA PFDKICYIGC GVTTGIGAVI 190 200 210 220 230 240 NTAKVEIGAK AVVFGLGGIG LNVLQGLRLA GADMIIGVDL NDDKKPMAEH FGMTHFINPK 250 260 270 280 290 300 NCENVVQEIV NLTKTPFDQI GGADYSFDCT GNVKVMRDAL ECTHRGWGQS IIIGVAPAGA 310 320 330 340 350 360 EISTRPFQLV TGRVWKGTAF GGARGRTDVP QIVDWYMDGK IEIDPMITHT LSLDDINKGF 370 DLMHAGESIR SVVLY

References

[1]

"Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth." Ras J., van Ophem P.W., Reijnders W.N.M., van Spanning R.J.M., Duine J.A., Stouthamer A.H., Harms N. J. Bacteriol. 177:247-251(1995) [PubMed: 7798140] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U34346 Genomic DNA. Translation: AAC44551.1. L36327 Genomic DNA. Translation: AAA65962.1.
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
ModBase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MON-4081.
BRENDA	1.1.1.284. 59.
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

FADH_PARDE

Accession

Primary (citable) accession number: P45382

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 52 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)