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P80040

- MDH_CHLAA

UniProt

P80040 - MDH_CHLAA

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Protein
Malate dehydrogenase
Gene
mdh, Caur_0900
Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Status
Reviewed - Annotation score: 4 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NAD
Binding sitei82 – 821Substrate
Binding sitei88 – 881Substrate
Binding sitei95 – 951NAD By similarity
Binding sitei120 – 1201Substrate By similarity
Binding sitei151 – 1511Substrate
Active sitei175 – 1751Proton acceptor By similarity
Binding sitei175 – 1751Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146NADUniRule annotation
Nucleotide bindingi118 – 1203NADUniRule 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

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciCAUR324602:GIXU-910-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
Ordered Locus Names:Caur_0900
OrganismiChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Taxonomic identifieri324602 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
ProteomesiUP000002008: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871T → C: Forms an intersubunit disulfide bridge, which makes the enzyme more resistant to thermal denaturation. The mutation does not alter the quaternary structure of the enzyme.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Malate dehydrogenaseUniRule annotation
PRO_0000113447Add
BLAST

Interactioni

Subunit structurei

Homotetramer (active enzyme); homodimer and homotrimer at temperatures lower than 55 degrees Celsius (inactive forms).3 Publications

Protein-protein interaction databases

STRINGi324602.Caur_0900.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Helixi12 – 2312
Beta strandi27 – 326
Beta strandi34 – 374
Helixi38 – 4710
Helixi50 – 534
Beta strandi59 – 635
Helixi65 – 684
Beta strandi72 – 765
Helixi90 – 10617
Helixi107 – 1093
Beta strandi114 – 1174
Beta strandi119 – 1213
Helixi122 – 13312
Helixi137 – 1393
Beta strandi140 – 1423
Helixi145 – 16016
Helixi164 – 1663
Beta strandi167 – 1693
Beta strandi172 – 1754
Helixi176 – 1783
Helixi183 – 1853
Beta strandi186 – 1883
Helixi193 – 1953
Helixi199 – 21012
Helixi212 – 2209
Beta strandi221 – 2233
Helixi227 – 24115
Beta strandi246 – 25611
Helixi257 – 2593
Beta strandi261 – 27212
Beta strandi275 – 2795
Helixi286 – 30621

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUYX-ray2.20A/C1-309[»]
1UR5X-ray1.75A/C1-309[»]
1UXGX-ray1.90A/B1-309[»]
1UXHX-ray2.10A/B1-309[»]
1UXIX-ray2.10A/B1-309[»]
1UXJX-ray1.75A/C1-309[»]
1UXKX-ray1.80A/C1-309[»]
4CL3X-ray1.70A/D1-309[»]
ProteinModelPortaliP80040.
SMRiP80040. Positions 2-309.

Miscellaneous databases

EvolutionaryTraceiP80040.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213794.
KOiK00024.
OrthoDBiEOG6091FG.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPiMF_00487. Malate_dehydrog_3.
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.
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01763. MalateDH_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P80040-1 [UniParc]FASTAAdd to Basket

« Hide

MRKKISIIGA GFVGSTTAHW LAAKELGDIV LLDFVEGVPQ GKALDLYEAS    50
PIEGFDVRVT GTNNYADTAN SDVIVVTSGA PRKPGMSRED LIKVNADITR 100
ACISQAAPLS PNAVIIMVNN PLDAMTYLAA EVSGFPKERV IGQAGVLDAA 150
RYRTFIAMEA GVSVEDVQAM LMGGHGDEMV PLPRFSTISG IPVSEFIAPD 200
RLAQIVERTR KGGGEIVNLL KTGSAYYAPA AATAQMVEAV LKDKKRVMPV 250
AAYLTGQYGL NDIYFGVPVI LGAGGVEKIL ELPLNEEEMA LLNASAKAVR 300
ATLDTLKSL 309
Length:309
Mass (Da):32,751
Last modified:March 18, 2008 - v3
Checksum:iAE1BACC5D5B36331
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341F → I in CAA61436. 1 Publication
Sequence conflicti34 – 341F → I1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89038 Genomic DNA. Translation: CAA61436.1.
CP000909 Genomic DNA. Translation: ABY34133.1.
RefSeqiYP_001634522.1. NC_010175.1.

Genome annotation databases

EnsemblBacteriaiABY34133; ABY34133; Caur_0900.
GeneIDi5827960.
KEGGicau:Caur_0900.
PATRICi21412507. VBIChlAur28763_1031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89038 Genomic DNA. Translation: CAA61436.1 .
CP000909 Genomic DNA. Translation: ABY34133.1 .
RefSeqi YP_001634522.1. NC_010175.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GUY X-ray 2.20 A/C 1-309 [» ]
1UR5 X-ray 1.75 A/C 1-309 [» ]
1UXG X-ray 1.90 A/B 1-309 [» ]
1UXH X-ray 2.10 A/B 1-309 [» ]
1UXI X-ray 2.10 A/B 1-309 [» ]
1UXJ X-ray 1.75 A/C 1-309 [» ]
1UXK X-ray 1.80 A/C 1-309 [» ]
4CL3 X-ray 1.70 A/D 1-309 [» ]
ProteinModelPortali P80040.
SMRi P80040. Positions 2-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 324602.Caur_0900.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABY34133 ; ABY34133 ; Caur_0900 .
GeneIDi 5827960.
KEGGi cau:Caur_0900.
PATRICi 21412507. VBIChlAur28763_1031.

Phylogenomic databases

eggNOGi COG0039.
HOGENOMi HOG000213794.
KOi K00024.
OrthoDBi EOG6091FG.

Enzyme and pathway databases

BioCyci CAUR324602:GIXU-910-MONOMER.

Miscellaneous databases

EvolutionaryTracei P80040.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPi MF_00487. Malate_dehydrog_3.
InterProi IPR001557. 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 ]
PANTHERi PTHR11540. PTHR11540. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000102. Lac_mal_DH. 1 hit.
PRINTSi PR00086. LLDHDRGNASE.
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01763. MalateDH_bact. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Malate dehydrogenase from the green gliding bacterium Chloroflexus aurantiacus is phylogenetically related to lactic dehydrogenases."
    Synstad B., Emmerhoff O., Sirevag R.
    Arch. Microbiol. 165:346-353(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29366 / DSM 635 / J-10-fl.
  3. "Malate dehydrogenase from the thermophilic green bacterium Chloroflexus aurantiacus: purification, molecular weight, amino acid composition, and partial amino acid sequence."
    Rolstad A.K., Howland E., Sirevag R.
    J. Bacteriol. 170:2947-2953(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-35, SUBUNIT.
  4. "Structural basis for thermophilic protein stability: structures of thermophilic and mesophilic malate dehydrogenases."
    Dalhus B., Saarinen M., Sauer U.H., Eklund P., Johansson K., Karlsson A., Ramaswamy S., Bjoerk A., Synstad B., Naterstad K., Sirevaag R., Eklund H.
    J. Mol. Biol. 318:707-721(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-306 IN COMPLEX WITH NAD, SUBUNIT.
  5. "Stabilization of a tetrameric malate dehydrogenase by introduction of a disulfide bridge at the dimer-dimer interface."
    Bjoerk A., Dalhus B., Mantzilas D., Eijsink V.G.H., Sirevaag R.
    J. Mol. Biol. 334:811-821(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF MUTANT CYS-187 IN COMPLEX WITH NAD AND SUBSTRATE ANALOG, SUBUNIT.

Entry informationi

Entry nameiMDH_CHLAA
AccessioniPrimary (citable) accession number: P80040
Secondary accession number(s): A9WH38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: March 18, 2008
Last modified: September 3, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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