I6XB21 (I6XB21_MYCTU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Malate dehydrogenase HAMAP-Rule MF_01517 RuleBase RU004066
EC=1.1.1.37 HAMAP-Rule MF_01517 RuleBase RU004066

Gene names

Name:	mdh HAMAP-Rule MF_01517
ORF Names:	RVBD_1240 EMBL AFN49144.1

Organism

Mycobacterium tuberculosis H37Rv EMBL AFN49144.1

Taxonomic identifier

83332 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium tuberculosis

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. SAAS SAAS001252 HAMAP-Rule MF_01517
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. SAAS SAAS010945 HAMAP-Rule MF_01517 RuleBase RU004066
Subunit structure	Homodimer By similarity. SAAS SAAS010945 HAMAP-Rule MF_01517
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family. HAMAP-Rule MF_01517 RuleBase RU000421

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle SAAS SAAS010945 RuleBase RU000422 HAMAP-Rule MF_01517
Ligand	NAD SAAS SAAS010945 RuleBase RU000422 HAMAP-Rule MF_01517
Molecular function	Oxidoreductase HAMAP-Rule MF_01517 RuleBase RU004066
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
Regions
	Nucleotide binding	12 – 18	7	NAD By similarity HAMAP-Rule MF_01517
	Nucleotide binding	130 – 132	3	NAD By similarity HAMAP-Rule MF_01517
Sites
	Active site	188	1	Proton acceptor By similarity HAMAP-Rule MF_01517
	Binding site	93	1	Substrate By similarity HAMAP-Rule MF_01517
	Binding site	99	1	Substrate By similarity HAMAP-Rule MF_01517
	Binding site	106	1	NAD By similarity HAMAP-Rule MF_01517
	Binding site	113	1	NAD By similarity HAMAP-Rule MF_01517
	Binding site	132	1	Substrate By similarity HAMAP-Rule MF_01517
	Binding site	163	1	Substrate By similarity HAMAP-Rule MF_01517

Sequences

	Sequence		Length	Mass (Da)
	I6XB21 [UniParc]. Last modified October 3, 2012. Version 1. Checksum: 0A512659617F9C37	FASTA	329	34,322
	10 20 30 40 50 60 MSASPLKVAV TGAAGQIGYS LLFRLASGSL LGPDRPIELR LLEIEPALQA LEGVVMELDD 70 80 90 100 110 120 CAFPLLSGVE IGSDPQKIFD GVSLALLVGA RPRGAGMERS DLLEANGAIF TAQGKALNAV 130 140 150 160 170 180 AADDVRVGVT GNPANTNALI AMTNAPDIPR ERFSALTRLD HNRAISQLAA KTGAAVTDIK 190 200 210 220 230 240 KMTIWGNHSA TQYPDLFHAE VAGKNAAEVV NDQAWIEDEF IPTVAKRGAA IIDARGASSA 250 260 270 280 290 300 ASAASATIDA ARDWLLGTPA DDWVSMAVVS DGSYGVPEGL ISSFPVTTKG GNWTIVSGLE 310 320 IDEFSRGRID KSTAELADER SAVTELGLI

References

[1]

"The Genome Sequence of Mycobacterium tuberculosis H37Rv." The Broad Institute Genome Sequencing Platform, The Broad Institute Genome Sequencing Center for Infectious Disease Galagan J., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A. , Larimer J., McCowan C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B. Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: H37Rv EMBL AFN49144.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP003248 Genomic DNA. Translation: AFN49144.1.
RefSeq	NP_215756.1. NC_000962.3. YP_006514615.1. NC_018143.1.
3D structure databases
ProteinModelPortal	I6XB21.
SMR	I6XB21. Positions 4-329.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AFN49144; AFN49144; RVBD_1240.
GeneID	13319819. 887119.
KEGG	mtu:Rv1240. mtv:RVBD_1240.
Phylogenomic databases
KO	K00024.
OMA	AINDHAA.
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. IPR001252. Malate_DH_AS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

I6XB21_MYCTU

Accession

Primary (citable) accession number: I6XB21

Entry history

Integrated into UniProtKB/TrEMBL:	October 3, 2012
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 8 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)