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Protein

Malate dehydrogenase

Gene

mdh

Organism
Brucella abortus (strain 2308)
Status
Reviewed-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 annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei34NADUniRule annotation1
Binding sitei83SubstrateUniRule annotation1
Binding sitei89SubstrateUniRule annotation1
Binding sitei96NADUniRule annotation1
Binding sitei121SubstrateUniRule annotation1
Binding sitei152SubstrateUniRule annotation1
Active sitei176Proton acceptorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15NADUniRule annotation6
Nucleotide bindingi119 – 121NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenaseUniRule annotation (EC:1.1.1.37UniRule annotation)
Gene namesi
Name:mdhUniRule annotation
Ordered Locus Names:BAB1_1927
OrganismiBrucella abortus (strain 2308)
Taxonomic identifieri359391 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000002719 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002419431 – 320Malate dehydrogenaseAdd BLAST320

Proteomic databases

PRIDEiQ2YLR9.

Structurei

Secondary structure

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Helixi13 – 24Combined sources12
Beta strandi29 – 33Combined sources5
Beta strandi35 – 38Combined sources4
Helixi39 – 54Combined sources16
Beta strandi60 – 65Combined sources6
Helixi66 – 69Combined sources4
Beta strandi73 – 77Combined sources5
Helixi91 – 110Combined sources20
Beta strandi115 – 118Combined sources4
Helixi123 – 134Combined sources12
Helixi138 – 140Combined sources3
Beta strandi141 – 143Combined sources3
Helixi146 – 161Combined sources16
Helixi165 – 167Combined sources3
Beta strandi172 – 174Combined sources3
Helixi177 – 179Combined sources3
Beta strandi180 – 182Combined sources3
Helixi184 – 186Combined sources3
Helixi194 – 199Combined sources6
Helixi205 – 216Combined sources12
Helixi218 – 226Combined sources9
Beta strandi227 – 229Combined sources3
Helixi233 – 247Combined sources15
Beta strandi252 – 262Combined sources11
Helixi263 – 265Combined sources3
Beta strandi267 – 278Combined sources12
Beta strandi281 – 285Combined sources5
Helixi292 – 315Combined sources24
Helixi317 – 319Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GVHX-ray2.30A/B/C/D1-320[»]
3GVIX-ray2.25A/B/C/D/E/F1-320[»]
ProteinModelPortaliQ2YLR9.
SMRiQ2YLR9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2YLR9.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 3 family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000213794.
KOiK00024.
OMAiMDLMQTA.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00487. Malate_dehydrog_3. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2YLR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARNKIALIG SGMIGGTLAH LAGLKELGDV VLFDIAEGTP QGKGLDIAES
60 70 80 90 100
SPVDGFDAKF TGANDYAAIE GADVVIVTAG VPRKPGMSRD DLLGINLKVM
110 120 130 140 150
EQVGAGIKKY APEAFVICIT NPLDAMVWAL QKFSGLPAHK VVGMAGVLDS
160 170 180 190 200
ARFRYFLSEE FNVSVEDVTV FVLGGHGDSM VPLARYSTVA GIPLPDLVKM
210 220 230 240 250
GWTSQDKLDK IIQRTRDGGA EIVGLLKTGS AFYAPAASAI QMAESYLKDK
260 270 280 290 300
KRVLPVAAQL SGQYGVKDMY VGVPTVIGAN GVERIIEIDL DKDEKAQFDK
310 320
SVASVAGLCE ACIGIAPSLK
Length:320
Mass (Da):33,704
Last modified:December 20, 2005 - v1
Checksum:iC212BA88F0241677
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM040264 Genomic DNA. Translation: CAJ11883.1.
RefSeqiWP_002964995.1. NZ_KN046823.1.

Genome annotation databases

EnsemblBacteriaiCAJ11883; CAJ11883; BAB1_1927.
GeneIDi3788794.
KEGGibmf:BAB1_1927.
PATRICi17846933. VBIBruMel86222_2007.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM040264 Genomic DNA. Translation: CAJ11883.1.
RefSeqiWP_002964995.1. NZ_KN046823.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GVHX-ray2.30A/B/C/D1-320[»]
3GVIX-ray2.25A/B/C/D/E/F1-320[»]
ProteinModelPortaliQ2YLR9.
SMRiQ2YLR9.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ2YLR9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAJ11883; CAJ11883; BAB1_1927.
GeneIDi3788794.
KEGGibmf:BAB1_1927.
PATRICi17846933. VBIBruMel86222_2007.

Phylogenomic databases

HOGENOMiHOG000213794.
KOiK00024.
OMAiMDLMQTA.

Miscellaneous databases

EvolutionaryTraceiQ2YLR9.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00487. Malate_dehydrog_3. 1 hit.
InterProiIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR011275. Malate_DH_type3.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11540. PTHR11540. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000102. Lac_mal_DH. 1 hit.
PRINTSiPR00086. LLDHDRGNASE.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMDH_BRUA2
AccessioniPrimary (citable) accession number: Q2YLR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Brucella abortus strain 2308
    Brucella abortus (strain 2308): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.