Reviewed, UniProtKB/Swiss-Prot O74540 (FADH2_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative S-(hydroxymethyl)glutathione dehydrogenase 2
    EC=1.1.1.284
Alternative name(s):
    Glutathione-dependent formaldehyde dehydrogenase 2
      Short name=GSH-FDH 2
      Short name=FALDH 2
      Short name=FDH 2
      Short name=FLD 2
    EC=1.1.1.-

Gene names

ORF Names:

SPCC13B11.04c, SPCC777.01c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.
Cofactor	Binds 2 zinc ions per subunit By similarity.
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	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	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
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 – 380	380	Putative S-(hydroxymethyl)glutathione dehydrogenase 2		PRO_0000160784
Sites
	Metal binding	50	1	Zinc 1; catalytic By similarity
	Metal binding	72	1	Zinc 1; catalytic By similarity
	Metal binding	102	1	Zinc 2 By similarity
	Metal binding	105	1	Zinc 2 By similarity
	Metal binding	108	1	Zinc 2 By similarity
	Metal binding	116	1	Zinc 2 By similarity
	Metal binding	179	1	Zinc 1; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	O74540-1 [UniParc]. Last modified August 1, 1999. Version 2. Checksum: 2E39F0F347BBBC45	FASTA	380	40,712
	10 20 30 40 50 60 MQQSPTAGKI INCKAAVAWQ PAAPLSIENV QVFPPRVHEV RIKIVNSGVC HTDAYTLSGK 70 80 90 100 110 120 DPEGLFPVIL GHEGAGIVES VGPQVTTVQV GDPVIALYTP ECKTCKFCKS GKTNLCGRIR 130 140 150 160 170 180 TTQGKGLMPD GTSRFSCNGN TLLHFMGCST FSEYTVVADI SVVAIERLAP LDSVCLLGCG 190 200 210 220 230 240 ITTGYGAATI TADIKEGDSV AVFGLGSVGL AVIQGAVKKR AGRIFGIDVN PEKKNWAMSF 250 260 270 280 290 300 GATDFINPND LQSPIQDVLI HETDGGLDWT FDCTGNVHVM RSALEACHKG WGQSIVIGVA 310 320 330 340 350 360 AAGQEISTRP FQLVTGRVWR GCAFGGVKGR SQLPDLVKEY LDHKLEIDKY ITHRRPLKEI 370 380 NEAFTDMHNG NCIKTVLSIP

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAA21785.1.
PIR	T40965.
RefSeq	NP_588247.1.
3D structure databases
HSSP	HSSP built from PDB template 1M6H based on UniProtKB P11766.
ModBase	Search...
Genome annotation databases
GeneID	2538802.
KEGG	spo:SPCC13B11.04c.
NMPDR	fig|4896.1.peg.585.
Organism-specific databases
GeneDB_Spombe	SPCC13B11.04c.
Phylogenomic databases
OMA	KSFQAWL.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000484-MON.
BRENDA	1.1.1.284. 653.
Gene expression databases
ArrayExpress	O74540.
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

FADH2_SCHPO

Accession

Primary (citable) accession number: O74540

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	August 1, 1999
Last modified:	November 3, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)