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Q393V1

- MDH_BURS3

UniProt

Q393V1 - MDH_BURS3

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Protein

Malate dehydrogenase

Gene
mdh, Bcep18194_B2154
Organism
Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194))
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931Substrate By similarity
Binding sitei99 – 991Substrate By similarity
Binding sitei106 – 1061NAD By similarity
Binding sitei113 – 1131NAD By similarity
Binding sitei132 – 1321Substrate By similarity
Binding sitei163 – 1631Substrate By similarity
Active sitei188 – 1881Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 187NAD By similarity
Nucleotide bindingi130 – 1323NAD By similarity

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

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciBSP269483:GHLS-5573-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
Ordered Locus Names:Bcep18194_B2154
OrganismiBurkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194))
Taxonomic identifieri482957 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000002705: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 328327Malate dehydrogenaseUniRule annotationPRO_0000294381Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi269483.Bcep18194_B2154.

Structurei

3D structure databases

ProteinModelPortaliQ393V1.
SMRiQ393V1. Positions 3-325.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000220953.
KOiK00024.
OMAiNCLIASK.
OrthoDBiEOG6PP9Q2.

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.
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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q393V1-1 [UniParc]FASTAAdd to Basket

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MAKPAKRVAV TGAAGQIAYS LLFRIANGDL LGKDQPVILQ LLDLPQAQGA    50
VKGVVMELDD CAFPLLSGVV ITDDPKVAFK DADVALLVGA RPRSKGMERK 100
DLLSANAEIF TVQGAALNEV ASRDVKVLVV GNPANTNAYI AMKSAPDLPK 150
KNFTAMLRLD HNRALSQLAA KSGKPVASIE KLAVWGNHSP TMYPDFRFAT 200
AEGESLLKLI NDDVWNRDTF IPTVGKRGAA IIEARGLSSA ASAANAAIDH 250
VRDWVLGTNG KWVTMGIPSD GSYGIPEDII YGVPVVCENG EYKRIEGLEI 300
DAFSREKMDG TLAELLEERD GVAHLLKN 328
Length:328
Mass (Da):35,131
Last modified:November 22, 2005 - v1
Checksum:iA43D956A12C1FE86
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000152 Genomic DNA. Translation: ABB12265.1.
RefSeqiWP_011355748.1. NC_007511.1.
YP_372909.1. NC_007511.1.

Genome annotation databases

EnsemblBacteriaiABB12265; ABB12265; Bcep18194_B2154.
GeneIDi3753919.
KEGGibur:Bcep18194_B2154.
PATRICi19295211. VBIBurSp120713_6967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000152 Genomic DNA. Translation: ABB12265.1 .
RefSeqi WP_011355748.1. NC_007511.1.
YP_372909.1. NC_007511.1.

3D structure databases

ProteinModelPortali Q393V1.
SMRi Q393V1. Positions 3-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269483.Bcep18194_B2154.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB12265 ; ABB12265 ; Bcep18194_B2154 .
GeneIDi 3753919.
KEGGi bur:Bcep18194_B2154.
PATRICi 19295211. VBIBurSp120713_6967.

Phylogenomic databases

eggNOGi COG0039.
HOGENOMi HOG000220953.
KOi K00024.
OMAi NCLIASK.
OrthoDBi EOG6PP9Q2.

Enzyme and pathway databases

BioCyci BSP269483:GHLS-5573-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_01517. Malate_dehydrog_2.
InterProi 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 ]
PANTHERi PTHR23382. PTHR23382. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01759. MalateDH-SF1. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of chromosome 2 of Burkholderia sp. 383."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 383.

Entry informationi

Entry nameiMDH_BURS3
AccessioniPrimary (citable) accession number: Q393V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: November 22, 2005
Last modified: September 3, 2014
This is version 65 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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