B7FJQ4 (B7FJQ4_MEDTR) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Malate dehydrogenase RuleBase RU003405
EC=1.1.1.37 RuleBase RU003405

Gene names

ORF Names:

MTR_1g043040 EMBL AES60276.1

Organism

Medicago truncatula (Barrel medic) (Medicago tribuloides) EMBL ACJ84983.1

Taxonomic identifier

3880 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family. RuleBase RU000421

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle RuleBase RU003405
Ligand	NAD RuleBase RU003405
Molecular function	Oxidoreductase RuleBase RU003405
Gene Ontology (GO)
Biological_process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B7FJQ4 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: D0339B804C53C228	FASTA	332	35,560
	10 20 30 40 50 60 MAKDPVRVLV TGAAGQIGYA LVPMIARGVM LGPDQPVILH MLDIAPAAES LNGVKMELVD 70 80 90 100 110 120 AAFPLLKGVV ATTDVVEACT GVNIAVMVGG FPRKEGMERK DVMSKNVSIY KSQASALEKH 130 140 150 160 170 180 AAANCKVLVV ANPANTNALI LKEFAPSIPE RNISCLTRLD HNRALGQISE RLNVQVSDVK 190 200 210 220 230 240 NVIIWGNHSS TQYPDVNHAT VNTPAGEKPV RELVSDDAWL NGEFISTVQQ RGAAIIKARK 250 260 270 280 290 300 LSSALSAASA ACDHIRDWVL GTPQGTFVSM GVYSDGSYNV PSGLIYSFPV TCANGEWKIV 310 320 330 QGLSIDEFSR KKLDLTAEEL SEEKNLAYSC LS

References

[1]

"Medicago truncatula full length cdna cloning project." Moskal W., Chan A., Cheung F., Xiao Y., Town C.D. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.

[2]

"The Medicago genome provides insight into the evolution of rhizobial symbioses." Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K., Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Krishnakumar V. , Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A. Nature 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: A17 EMBL AES60276.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BT052321 mRNA. Translation: ACJ84983.1. CM001217 Genomic DNA. Translation: AES60276.1.
RefSeq	XP_003590025.1. XM_003589977.1.
UniGene	Mtr.5089.
3D structure databases
ProteinModelPortal	B7FJQ4.
ModBase	Search...
Proteomic databases
ProMEX	B7FJQ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	11430390.
KEGG	mtr:MTR_1g043040.
Phylogenomic databases
KO	K00025.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
InterPro	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]
PANTHER	PTHR23382. PTHR23382. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMs	TIGR01759. MalateDH-SF1. 1 hit. TIGR01758. MDH_euk_cyt. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B7FJQ4_MEDTR

Accession

Primary (citable) accession number: B7FJQ4

Entry history

Integrated into UniProtKB/TrEMBL:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	March 6, 2013
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)