P82177 (MDH_SHEON) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malate dehydrogenase
EC=1.1.1.37

Gene names

Name:	mdh
Ordered Locus Names:	SO_0770

Organism

Shewanella oneidensis (strain MR-1) [Reference proteome] [HAMAP]

Taxonomic identifier

211586 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella › Shewanella oneidensis

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01516
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01516
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.
Mass spectrometry	Molecular mass is 1734.8 Da from positions 3 - 21. Determined by ESI. Ref.2

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
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: HAMAP
Molecular_function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP nucleotide 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
	Chain	1 – 311	311	Malate dehydrogenase HAMAP-Rule MF_01516		PRO_0000113326
Regions
	Nucleotide binding	7 – 13	7	NAD By similarity
	Nucleotide binding	117 – 119	3	NAD By similarity
Sites
	Active site	177	1	Proton acceptor By similarity
	Binding site	34	1	NAD By similarity
	Binding site	81	1	Substrate By similarity
	Binding site	87	1	Substrate By similarity
	Binding site	94	1	NAD By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity
	Binding site	227	1	NAD By similarity
Experimental info
	Sequence conflict	13	1	Missing AA sequence Ref.2
	Sequence conflict	16	1	L → LG AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P82177 [UniParc]. Last modified November 15, 2002. Version 2. Checksum: 9D3F5E86A2500A1B	FASTA	311	32,137
	10 20 30 40 50 60 MKVAVLGAAG GIGQALALLL KTQLPAGSKL SLYDIAPVTP GVAVDLSHIP TAVEIKGFAG 70 80 90 100 110 120 EDPTPALVGA DVVLISAGVA RKPGMDRSDL FNINAGIVRN LIEKVAVTCP KALVGIITNP 130 140 150 160 170 180 VNTTVAIAAE VMKKAGVYDK NRLFGVTTLD VIRSETFIAE LKGLNVADVK INVIGGHSGV 190 200 210 220 230 240 TILPLLSQVE GVTFSDEEVA SLTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGMSLVR 250 260 270 280 290 300 GLQGEANVVE CAYVDGGSEH AEFFAQPVLL GKNGIEKVLP YGEVSAFEAN ARDSMLDTLK 310 GDIKLGVDFV K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis." Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C., DeBoy R.T. , Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C., Nealson K.H., Fraser C.M. Nat. Biotechnol. 20:1118-1123(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MR-1.
[2]	"Automated nanoflow liquid chromatography/tandem mass spectrometric identification of proteins from Shewanella putrefaciens separated by two-dimensional polyacrylamide gel electrophoresis." Devreese B., Vanrobaeys F., Van Beeumen J. Rapid Commun. Mass Spectrom. 15:50-56(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-21, MASS SPECTROMETRY. Strain: MR-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014299 Genomic DNA. Translation: AAN53846.1.
RefSeq	NP_716401.1. NC_004347.2.
3D structure databases
ProteinModelPortal	P82177.
SMR	P82177. Positions 1-310.
ModBase	Search...
Protein-protein interaction databases
STRING	211586.SO_0770.
Proteomic databases
PRIDE	P82177.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN53846; AAN53846; SO_0770.
GeneID	1168625.
KEGG	son:SO_0770.
PATRIC	23521213. VBISheOne101494_0740.
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000213792.
KO	K00024.
OMA	VEVKGFA.
ProtClustDB	PRK05086.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
HAMAP	MF_01516. Malate_dehydrog_1.
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. IPR010097. Malate_DH_type1. IPR023958. Malate_DH_type1_bac. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11540. PTHR11540. 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	TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_SHEON

Accession

Primary (citable) accession number: P82177

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 15, 2002
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program