Reviewed, UniProtKB/Swiss-Prot P36624 (DHSO_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative sorbitol dehydrogenase
    EC=1.1.1.14
Alternative name(s):
    L-iditol 2-dehydrogenase
    Protein tms1

Gene names

Name:	tms1
ORF Names:	SPBC1773.05c

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

General annotation (Comments)

Function	Suppresses growth arrest induced by a p53 tumor mutant in fission yeast.
Catalytic activity	L-iditol + NAD+ = L-sorbose + NADH.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to stress Inferred from expression pattern. Source: GeneDB_SPombe hexitol catabolic process Inferred by curator. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	L-iditol 2-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 – 360	360	Putative sorbitol dehydrogenase		PRO_0000160823
Sites
	Metal binding	42	1	Zinc; catalytic By similarity
	Metal binding	67	1	Zinc; catalytic By similarity
	Metal binding	68	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	P36624-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: ADEB3DDBA163224C	FASTA	360	38,851
	10 20 30 40 50 60 MAPAEKAFVL RKKMDTAIED RPGQTLTDDH QVKVAIKATG ICGSDVHYWK EGGIGDFILK 70 80 90 100 110 120 KPMILGHESA GVVVEVGKGV SSLKPGDPVA VEPGCVCRLC DYCRSGRYNL CPHMEFAATP 130 140 150 160 170 180 PYDGTLRTYY ITTEDFCTKL PKQISVEEGA LFEPMSVAVH AMTRGNLKCG SRVLVMGCGT 190 200 210 220 230 240 VGLLMMAVAK AYGAIDIVAV DASPSRVEFA QKYVGAKPFT PIAAKENESL PDYAQRYKQA 250 260 270 280 290 300 IIEKYGEFDF AVDATGVGIC IHTAVLALKR GGTFVQAGNG KPVIDFPINH IINYEINVLG 310 320 330 340 350 360 SFRYAHGCYK QSLFLVSNGL VDVKPLITHR FAFKDALKAY ETVASGEEGV LKVIIGGPDA

References

	« Hide 'large scale' referencesShow 'large scale' 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.
[2]	"Putative dehydrogenase tms1 suppresses growth arrest induced by a p53 tumour mutant in fission yeast." Wagner P., Grimaldi M., Jenkins J.R. Eur. J. Biochem. 217:731-736(1993) [PubMed: 8223615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-360. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA21910.1. X74422 Genomic DNA. Translation: CAA52443.1. Different initiation.
PIR	S35981. T39670.
RefSeq	NP_595120.1.
3D structure databases
HSSP	HSSP built from PDB template 1E3J based on UniProtKB O96496.
ModBase	Search...
Genome annotation databases
GeneID	2540119.
KEGG	spo:SPBC1773.05c.
NMPDR	fig|4896.1.peg.986.
Organism-specific databases
GeneDB_Spombe	SPBC1773.05c.
Phylogenomic databases
OMA	P36624. HNANFCY.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-003219-MON.
BRENDA	1.1.1.14. 653.
Gene expression databases
ArrayExpress	P36624.
Family and domain databases
InterPro	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]
ProDom	PD040557. GroES_related. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHSO_SCHPO

Accession

Primary (citable) accession number: P36624

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 11, 2001
Last modified:	June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)