Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Malate dehydrogenase

Gene

mdh

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate.UniRule annotation

Catalytic activityi

(S)-malate + NAD+ = oxaloacetate + NADH.UniRule annotationSAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931SubstrateUniRule annotation
Binding sitei99 – 991SubstrateUniRule annotation
Binding sitei106 – 1061NADUniRule annotation
Binding sitei113 – 1131NADUniRule annotation
Binding sitei132 – 1321SubstrateUniRule annotation
Binding sitei163 – 1631SubstrateUniRule annotation
Active sitei188 – 1881Proton acceptorUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 187NADUniRule annotation
Nucleotide bindingi130 – 1323NADUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Keywords - Ligandi

NADUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenaseUniRule annotation (EC:1.1.1.37UniRule annotation)
Gene namesi
Name:mdhUniRule annotation
Ordered Locus Names:RVBD_1240Imported
ORF Names:LH57_06785Imported, P425_01288Imported
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)Imported
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000003123: Chromosome

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TVOX-ray1.50A/B2-329[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 2 family.UniRule annotation

Phylogenomic databases

KOiK00024.
OMAiAFKDTDY.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
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.
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.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

I6XB21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASPLKVAV TGAAGQIGYS LLFRLASGSL LGPDRPIELR LLEIEPALQA
60 70 80 90 100
LEGVVMELDD CAFPLLSGVE IGSDPQKIFD GVSLALLVGA RPRGAGMERS
110 120 130 140 150
DLLEANGAIF TAQGKALNAV AADDVRVGVT GNPANTNALI AMTNAPDIPR
160 170 180 190 200
ERFSALTRLD HNRAISQLAA KTGAAVTDIK KMTIWGNHSA TQYPDLFHAE
210 220 230 240 250
VAGKNAAEVV NDQAWIEDEF IPTVAKRGAA IIDARGASSA ASAASATIDA
260 270 280 290 300
ARDWLLGTPA DDWVSMAVVS DGSYGVPEGL ISSFPVTTKG GNWTIVSGLE
310 320
IDEFSRGRID KSTAELADER SAVTELGLI
Length:329
Mass (Da):34,322
Last modified:October 3, 2012 - v1
Checksum:i0A512659617F9C37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003248 Genomic DNA. Translation: AFN49144.1.
CP009480 Genomic DNA. Translation: AIR13986.1.
JLDD01000013 Genomic DNA. Translation: KBJ36253.1.
RefSeqiNP_215756.1. NC_000962.3.
YP_006514615.1. NC_018143.2.

Genome annotation databases

EnsemblBacteriaiAFN49144; AFN49144; RVBD_1240.
KBJ36253; KBJ36253; P425_01288.
GeneIDi13319819.
887119.
KEGGimtu:Rv1240.
mtv:RVBD_1240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003248 Genomic DNA. Translation: AFN49144.1.
CP009480 Genomic DNA. Translation: AIR13986.1.
JLDD01000013 Genomic DNA. Translation: KBJ36253.1.
RefSeqiNP_215756.1. NC_000962.3.
YP_006514615.1. NC_018143.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4TVOX-ray1.50A/B2-329[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFN49144; AFN49144; RVBD_1240.
KBJ36253; KBJ36253; P425_01288.
GeneIDi13319819.
887119.
KEGGimtu:Rv1240.
mtv:RVBD_1240.

Phylogenomic databases

KOiK00024.
OMAiAFKDTDY.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_01517. Malate_dehydrog_2.
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.
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.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37RvImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.
  3. "Structures of citrate synthase and malate dehydrogenase of mycobacterium tuberculosis."
    Ferraris D.M., Spallek R., Oehlmann W., Singh M., Rizzi M.
    Proteins 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-329.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.
  5. "Phylogenetic analysis of Mycobacterial species using whole genome sequences."
    Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J., Monaco A., King S., Sohrabi A.
    Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.

Entry informationi

Entry nameiI6XB21_MYCTU
AccessioniPrimary (citable) accession number: I6XB21
Entry historyi
Integrated into UniProtKB/TrEMBL: October 3, 2012
Last sequence update: October 3, 2012
Last modified: March 4, 2015
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.