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O48905

- MDHC_MEDSA

UniProt

O48905 - MDHC_MEDSA

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Protein
Malate dehydrogenase, cytoplasmic
Gene
CMDH
Organism
Medicago sativa (Alfalfa)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931Substrate By similarity
Binding sitei99 – 991Substrate By similarity
Binding sitei106 – 1061NAD By similarity
Binding sitei113 – 1131NAD By similarity
Binding sitei132 – 1321Substrate By similarity
Binding sitei163 – 1631Substrate By similarity
Active sitei188 – 1881Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 187NAD By similarity
Nucleotide bindingi130 – 1323NAD By similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. malate metabolic process Source: InterPro
  3. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciARA:MONOMER-17412.
MetaCyc:MONOMER-17412.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase, cytoplasmic (EC:1.1.1.37)
Gene namesi
Name:CMDH
OrganismiMedicago sativa (Alfalfa)
Taxonomic identifieri3879 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeTrifolieaeMedicago

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Malate dehydrogenase, cytoplasmic
PRO_0000113416Add
BLAST

Proteomic databases

PRIDEiO48905.
ProMEXiO48905.

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliO48905.
SMRiO48905. Positions 4-332.

Family & Domainsi

Sequence similaritiesi

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.
IPR001252. Malate_DH_AS.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR23382. PTHR23382. 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.
TIGRFAMsiTIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O48905-1 [UniParc]FASTAAdd to Basket

« Hide

MAKDPVRVLV TGAAGQIGYA LVPMIARGVM LGPDQPVILH MLDIAPAAES    50
LNGVKMELVD AAFPLLKGVV ATTDVVEACT GVNIAVMVGG FPRKEGMERK 100
DVMSKNVSIY KSQASALEKH AAANCKVLVV ANPANTNALI LKEFAPSIPE 150
RNISCLTRLD HNRALGQISE RLNVQVSDVK NVIIWGNHSS TQYPDVNHAT 200
VNTPAGEKPV RQLVSDDAWL NGEFISTVQQ RGAAIIKARK LSSALSAASA 250
ACDHIRDWVL GTPQGTFVSM GVYSDGSYNV PSGLIYSFPV TCANGEWKIV 300
QGLSIDEFSR KKLDLTAEEL TEEKNLAHSC LS 332
Length:332
Mass (Da):35,547
Last modified:June 1, 1998 - v1
Checksum:iD9F38F868DE3D628
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF020272 mRNA. Translation: AAB99756.1.
PIRiT09291.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF020272 mRNA. Translation: AAB99756.1 .
PIRi T09291.

3D structure databases

ProteinModelPortali O48905.
SMRi O48905. Positions 4-332.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi O48905.
ProMEXi O48905.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci ARA:MONOMER-17412.
MetaCyc:MONOMER-17412.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProi IPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR011274. Malate_DH_NAD-dep_euk.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR23382. PTHR23382. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01759. MalateDH-SF1. 1 hit.
TIGR01758. MDH_euk_cyt. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Alfalfa malate dehydrogenase (MDH): molecular cloning and characterization of five different forms reveals a unique nodule-enhanced MDH."
    Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P.
    Plant J. 15:173-184(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Saranac.
    Tissue: Root nodule.

Entry informationi

Entry nameiMDHC_MEDSA
AccessioniPrimary (citable) accession number: O48905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: February 19, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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