Q8PC25 (MDH_XANCP) 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:	XCC0928

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas campestris › Xanthomonas campestris pv. campestris

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome 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 – 328	328	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_0000113402
Regions
	Nucleotide binding	11 – 17	7	NAD By similarity
	Nucleotide binding	131 – 133	3	NAD By similarity
Sites
	Active site	189	1	Proton acceptor By similarity
	Binding site	94	1	Substrate By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	107	1	NAD By similarity
	Binding site	114	1	NAD By similarity
	Binding site	133	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PC25 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 0CC5DE99D0DD863F	FASTA	328	34,935
	10 20 30 40 50 60 MKAPVRVAVT GAAGQIGYAL LFRIASGEML GKDQPVILQL LELSNEKAQA ALKGVMMELE 70 80 90 100 110 120 DCAFPLLAGM VGTDDAEVAF KDIDVALLVG ARPRGPGMER KDLLLENAKI FTAQGAALNK 130 140 150 160 170 180 VAKRDVKVLV VGNPANTNAY IAMKSAPDLN PKNFTAMLRL DHNRALSQLS LKLGKPVGGI 190 200 210 220 230 240 EKLVVWGNHS PTMYPDYRFA TSDGASIGDA INDQEWNAGT FIPTVGKRGA AIIEARGLSS 250 260 270 280 290 300 AASAANAAID HVRDWVLGSN GKWVTMGVPS DGSYGIPEGV IFGFPVTTEN GQYTLVKDLP 310 320 IDDFSQKYID KTLAELEEER SGVSHLLG

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM40238.1.
RefSeq	NP_636314.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8PC25.
SMR	Q8PC25. Positions 2-328.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC0928.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM40238; AAM40238; XCC0928.
GeneID	1001478.
KEGG	xcc:XCC0928.
PATRIC	24072541. VBIXanCam115730_1000.
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000220953.
KO	K00024.
OMA	NCLIASK.
ProtClustDB	PRK05442.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
HAMAP	MF_01517. Malate_dehydrog_2.
InterPro	IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. 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.
PROSITE	PS00068. MDH. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_XANCP

Accession

Primary (citable) accession number: Q8PC25

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program