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P80040

- MDH_CHLAA

UniProt

P80040 - MDH_CHLAA

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Protein

Malate dehydrogenase

Gene

mdh

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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331NAD2 Publications
Binding sitei82 – 821Substrate
Binding sitei88 – 881Substrate
Binding sitei95 – 951NADBy similarity
Binding sitei120 – 1201SubstrateBy similarity
Binding sitei151 – 1511Substrate
Active sitei175 – 1751Proton acceptorBy similarity
Binding sitei175 – 1751Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146NAD2 Publications
Nucleotide bindingi118 – 1203NAD2 Publications

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 dehydrogenasePRO_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

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi12 – 2312Combined sources
Beta strandi27 – 326Combined sources
Beta strandi34 – 374Combined sources
Helixi38 – 4710Combined sources
Helixi50 – 534Combined sources
Beta strandi59 – 635Combined sources
Helixi65 – 684Combined sources
Beta strandi72 – 765Combined sources
Helixi90 – 10617Combined sources
Helixi107 – 1093Combined sources
Beta strandi114 – 1174Combined sources
Beta strandi119 – 1213Combined sources
Helixi122 – 13312Combined sources
Helixi137 – 1393Combined sources
Beta strandi140 – 1423Combined sources
Helixi145 – 16016Combined sources
Helixi164 – 1663Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi172 – 1754Combined sources
Helixi176 – 1783Combined sources
Helixi183 – 1853Combined sources
Beta strandi186 – 1883Combined sources
Helixi193 – 1953Combined sources
Helixi199 – 21012Combined sources
Helixi212 – 2209Combined sources
Beta strandi221 – 2233Combined sources
Helixi227 – 24115Combined sources
Beta strandi246 – 25611Combined sources
Helixi257 – 2593Combined sources
Beta strandi261 – 27212Combined sources
Beta strandi275 – 2795Combined sources
Helixi286 – 30621Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80040.

Family & Domainsi

Sequence similaritiesi

Belongs to the LDH/MDH superfamily. MDH type 3 family.Curated

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213794.
InParanoidiP80040.
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

        10         20         30         40         50
MRKKISIIGA GFVGSTTAHW LAAKELGDIV LLDFVEGVPQ GKALDLYEAS
60 70 80 90 100
PIEGFDVRVT GTNNYADTAN SDVIVVTSGA PRKPGMSRED LIKVNADITR
110 120 130 140 150
ACISQAAPLS PNAVIIMVNN PLDAMTYLAA EVSGFPKERV IGQAGVLDAA
160 170 180 190 200
RYRTFIAMEA GVSVEDVQAM LMGGHGDEMV PLPRFSTISG IPVSEFIAPD
210 220 230 240 250
RLAQIVERTR KGGGEIVNLL KTGSAYYAPA AATAQMVEAV LKDKKRVMPV
260 270 280 290 300
AAYLTGQYGL NDIYFGVPVI LGAGGVEKIL ELPLNEEEMA LLNASAKAVR

ATLDTLKSL
Length:309
Mass (Da):32,751
Last modified:March 18, 2008 - v3
Checksum:iAE1BACC5D5B36331
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341F → I in CAA61436. (PubMed:8661927)Curated
Sequence conflicti34 – 341F → I(PubMed:3133356)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P80040.
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: November 26, 2014
This is version 118 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