Reviewed, UniProtKB/Swiss-Prot O94521 (PLR2_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable pyridoxal reductase 2
      Short name=PL reductase 2
      Short name=PL-red 2
    EC=1.1.1.65

Gene names

ORF Names:

SPCC1281.04

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	333 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP+ By similarity.
Catalytic activity	Pyridoxine + NADP+ = pyridoxal + NADPH.
Subcellular location	Cytoplasm Ref.2.
Sequence similarities	Belongs to the aldo/keto reductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to stress Inferred from expression pattern. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	pyridoxine 4-dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	Probable pyridoxal reductase 2		PRO_0000310315
Sites
	Active site	52	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	O94521-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: D69C0BEE8735E0F2	FASTA	333	36,844
	10 20 30 40 50 60 MPIVNGFKVG PIGLGLMGLT WRPKQTPIKQ AFELMNYALS QGSNYWNAGE FYGINPPTAN 70 80 90 100 110 120 LDLLADYFEK YPKNADKVFL SVKGGTDFKT LAPHGDPESV TKSVKNALTR LRGKKKLDLF 130 140 150 160 170 180 QCARVDHKVP IETTMKALKA FVDSGEISCV GLSEASAESI KRALAIVPIA AVETEYSLFS 190 200 210 220 230 240 RDIEKNGILD TCTQLSIPII AYAPFCHGLL TGRVKTAEDL KDFIKAFPFL RNMDKFNPKV 250 260 270 280 290 300 FEKNIPFLKA VEQLAQKFGM SMPEFALNFI IANGKGMIIP IPGSTTVQRA ESNLSALKKS 310 320 330 LSSEQLEEAK KVLDKHQIFG LRYNKQLEST LSI

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]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA22825.1.
PIR	T40923.
RefSeq	NP_588168.1.
3D structure databases
SMR	O94521. Positions 5-316.
ModBase	Search...
Genome annotation databases
GeneID	2539165.
KEGG	spo:SPCC1281.04.
NMPDR	fig|4896.1.peg.506.
Organism-specific databases
GeneDB_Spombe	SPCC1281.04.
Phylogenomic databases
eggNOG	fuNOG05889.
HOGENOM	HBG605727.
OMA	YPEYKSK.
OrthoDB	EOG9K0S4K.
PhylomeDB	O94521.
Enzyme and pathway databases
BRENDA	1.1.1.65. 653.
Gene expression databases
ArrayExpress	O94521.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. [Graphical view]
Gene3D	G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. False negative. PS00062. ALDOKETO_REDUCTASE_2. False negative. PS00063. ALDOKETO_REDUCTASE_3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLR2_SCHPO

Accession

Primary (citable) accession number: O94521

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 13, 2007
Last sequence update:	May 1, 1999
Last modified:	January 19, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)