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Protein

Malate dehydrogenase, mitochondrial

Gene

MDH1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611NADBy similarity
Binding sitei109 – 1091SubstrateBy similarity
Binding sitei115 – 1151SubstrateBy similarity
Binding sitei122 – 1221NADBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Binding sitei181 – 1811SubstrateBy similarity
Active sitei205 – 2051Proton acceptorBy similarity
Binding sitei254 – 2541NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 417NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).
REACT_300459. Gluconeogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, mitochondrial (EC:1.1.1.37)
Gene namesi
Name:MDH1
ORF Names:SPCC306.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC306.08c.
PomBaseiSPCC306.08c.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: PomBase
  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 341Malate dehydrogenase, mitochondrialPRO_0000310436
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ9Y7R8.
PaxDbiQ9Y7R8.
PRIDEiQ9Y7R8.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi275349. 1 interaction.
MINTiMINT-4718476.
STRINGi4896.SPCC306.08c-1.

Structurei

3D structure databases

ProteinModelPortaliQ9Y7R8.
SMRiQ9Y7R8. Positions 30-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213792.
InParanoidiQ9Y7R8.
KOiK00026.
OMAiQGQKNVI.
OrthoDBiEOG7GJ6Q7.
PhylomeDBiQ9Y7R8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010097. Malate_DH_type1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y7R8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFAKVAFKNF TPLKSIAPRS FSTTSSRAFK VAVLGAGGGI GQPLSMLLKL
60 70 80 90 100
NDKVSELALF DIRGAPGVAA DIGHINTTSN VVGYAPDDKG LEKALNGADV
110 120 130 140 150
VIIPAGVPRK PGMTRDDLFA TNASIVRDLA FAAGETCPEA KYLVVTNPVN
160 170 180 190 200
STVPIFKKAL ERVGVHQPKH LFGVTTLDSV RASRFTSQVT NGKAELLHIP
210 220 230 240 250
VVGGHSGATI VPLLSQGGVE LTGEKRDALI HRIQFGGDEV VKAKAGAGSA
260 270 280 290 300
TLSMAYAGAR MASSVLRALA GESGVEECTF VESPLYKDQG IDFFASRVTL
310 320 330 340
GKDGVDTIHP VGKINDYEES LLKVALGELK KSITKGEQFV A
Length:341
Mass (Da):35,787
Last modified:November 1, 1999 - v1
Checksum:i4681EBFD2B1F7716
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAB41656.1.
PIRiT41286.
RefSeqiNP_587816.1. NM_001022809.2.

Genome annotation databases

EnsemblFungiiSPCC306.08c.1; SPCC306.08c.1:pep; SPCC306.08c.
GeneIDi2538766.
KEGGispo:SPCC306.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAB41656.1.
PIRiT41286.
RefSeqiNP_587816.1. NM_001022809.2.

3D structure databases

ProteinModelPortaliQ9Y7R8.
SMRiQ9Y7R8. Positions 30-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275349. 1 interaction.
MINTiMINT-4718476.
STRINGi4896.SPCC306.08c-1.

Proteomic databases

MaxQBiQ9Y7R8.
PaxDbiQ9Y7R8.
PRIDEiQ9Y7R8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC306.08c.1; SPCC306.08c.1:pep; SPCC306.08c.
GeneIDi2538766.
KEGGispo:SPCC306.08c.

Organism-specific databases

EuPathDBiFungiDB:SPCC306.08c.
PomBaseiSPCC306.08c.

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213792.
InParanoidiQ9Y7R8.
KOiK00026.
OMAiQGQKNVI.
OrthoDBiEOG7GJ6Q7.
PhylomeDBiQ9Y7R8.

Enzyme and pathway databases

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).
REACT_300459. Gluconeogenesis.

Miscellaneous databases

NextBioi20799950.
PROiQ9Y7R8.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR010097. Malate_DH_type1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01772. MDH_euk_gproteo. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMDHM_SCHPO
AccessioniPrimary (citable) accession number: Q9Y7R8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 1, 1999
Last modified: May 27, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.