Q9C1X2 (YN53_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative D-lactate dehydrogenase C713.03, mitochondrial
EC=1.1.2.4

Gene names

ORF Names:

SPBC713.03

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	(R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c.
Cofactor	FAD Potential.
Subcellular location	Mitochondrion matrix Ref.2.
Sequence similarities	Belongs to the FAD-binding oxidoreductase/transferase type 4 family. Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	generation of precursor metabolites and energy Non-traceable author statement. Source: GeneDB_Spombe lactate metabolic process Inferred by curator. Source: GeneDB_Spombe
Cellular component	mitochondrial matrix Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Molecular function	D-lactate dehydrogenase (cytochrome) activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 526		Putative D-lactate dehydrogenase C713.03, mitochondrial		PRO_0000317236
Regions
	Domain	93 – 272	180	FAD-binding PCMH-type

Sequences

	Sequence		Length	Mass (Da)
	Q9C1X2 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 00FAF5ABA81EBC11	FASTA	526	58,473
	10 20 30 40 50 60 MHSLQCRRVI PFGKLSLSLH APRNALRFVH KPAFTFESYK SLHRDPKYAK LSEQDVQVFK 70 80 90 100 110 120 SIIGKDGSLI DGLDKSTDPA DLDAFNIDWM NKYRGKTQLA LKPKTTQQVS EILKYCNQKK 130 140 150 160 170 180 LAVVPQGGNT GLVGGSVPVF DEIVLNLGLM NQIHTFDEIS GVITLDSGVI LENADNFLAE 190 200 210 220 230 240 KGYMFPLDLG AKGSCQVGGC AATAAGGLRL LRYGSLHGSI LGMEAVLPDG TILDNLVTLR 250 260 270 280 290 300 KDNTGLDIKQ LFIGSEGYLG VITKLSVICP KRPSSTNVAF FGVPSYENVL KAFSETRSHL 310 320 330 340 350 360 TEILSAFELM DNTSQTLVDK YSGTQRPLED EHPFYVLVET QGSNKEHDEQ KITALVEDLL 370 380 390 400 410 420 EKEIISDGVL AQDESQLRVL WERREGITEC LAKAGSGVYK YDVSLPLPVL YDLVNDTKKR 430 440 450 460 470 480 LIEFNLLDDT PEHPVIDVVG FGHMGDGNLH LNIAVRQFDK RVEKCLEPWV YEWVSRHRGS 490 500 510 520 ISAEHGLGLL KKPFVGYSKS KEMIHLMKTL KNVFDPNGIM LPYKYV

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: 972 / ATCC 24843.

[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	CU329671 Genomic DNA. Translation: CAC22604.1.
RefSeq	NP_595342.1. NM_001021250.1.
3D structure databases
ProteinModelPortal	Q9C1X2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9C1X2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC713.03.1; SPBC713.03.1:pep; SPBC713.03.
GeneID	2541151.
KEGG	spo:SPBC713.03.
NMPDR	fig|4896.1.peg.1208.
Organism-specific databases
GeneDB_Spombe	SPBC713.03.
Phylogenomic databases
eggNOG	fuNOG04802.
GeneTree	EFGT00050000001281.
HOGENOM	HBG553036.
OMA	EPFVYEW.
OrthoDB	EOG4F4WKV.
Gene expression databases
ArrayExpress	Q9C1X2.
Family and domain databases
InterPro	IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016164. FAD-linked_Oxase-like_C. IPR016168. FAD-linked_Oxase_FAD-bd_sub2. IPR004113. FAD-linked_oxidase_C. IPR006094. Oxid_FAD_bind_N. IPR016171. Vanillyl_alc_oxidase_C-sub2. [Graphical view]
Gene3D	G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit. G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit. G3DSA:1.10.45.10. Vanillyl_alc_oxidase_C-sub2. 1 hit.
Pfam	PF02913. FAD-oxidase_C. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
SUPFAM	SSF55103. FAD-binding_2. 1 hit. SSF56176. FAD-binding_2. 1 hit.
PROSITE	PS51387. FAD_PCMH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YN53_SCHPO

Accession

Primary (citable) accession number: Q9C1X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	June 1, 2001
Last modified:	December 14, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program