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P80039

- MDH_CHLTE

UniProt

P80039 - MDH_CHLTE

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Protein

Malate dehydrogenase

Gene

mdh

Organism
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
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 sitei32 – 321NAD1 Publication
Binding sitei81 – 811SubstrateBy similarity
Binding sitei87 – 871SubstrateBy similarity
Binding sitei94 – 941NAD1 Publication
Binding sitei119 – 1191SubstrateBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Active sitei174 – 1741Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 126NAD1 Publication
Nucleotide bindingi117 – 1193NAD1 Publication

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

BioCyciCTEP194439:GHN0-1546-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
Ordered Locus Names:CT1507
OrganismiChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Taxonomic identifieri194439 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum
ProteomesiUP000001007: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Malate dehydrogenasePRO_0000113448Add
BLAST

Interactioni

Subunit structurei

Homotetramer; arranged as a dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi194439.CT1507.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi10 – 2112
Beta strandi26 – 316
Beta strandi33 – 364
Helixi37 – 4610
Helixi49 – 524
Beta strandi57 – 626
Helixi64 – 674
Beta strandi71 – 755
Helixi92 – 10514
Turni106 – 1083
Beta strandi113 – 1164
Beta strandi118 – 1203
Helixi121 – 13212
Helixi136 – 1383
Beta strandi139 – 1424
Helixi144 – 15916
Helixi163 – 1653
Beta strandi166 – 1727
Helixi175 – 1773
Beta strandi178 – 18710
Helixi192 – 1943
Helixi198 – 20912
Helixi211 – 2199
Beta strandi220 – 2223
Helixi226 – 24015
Beta strandi245 – 25511
Helixi256 – 2583
Beta strandi260 – 27112
Beta strandi274 – 2785
Helixi285 – 30420

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GUZX-ray2.00A/B/C/D1-71[»]
1GV0X-ray2.50A/B1-310[»]
ProteinModelPortaliP80039.
SMRiP80039. Positions 1-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80039.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0039.
HOGENOMiHOG000213794.
KOiK00024.
OMAiYGQNDIC.
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.

P80039-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKITVIGAGN VGATTAFRLA EKQLARELVL LDVVEGIPQG KALDMYESGP
60 70 80 90 100
VGLFDTKVTG SNDYADTANS DIVVITAGLP RKPGMTREDL LSMNAGIVRE
110 120 130 140 150
VTGRIMEHSK NPIIVVVSNP LDIMTHVAWQ KSGLPKERVI GMAGVLDSAR
160 170 180 190 200
FRSFIAMELG VSMQDVTACV LGGHGDAMVP VVKYTTVAGI PVADLISAER
210 220 230 240 250
IAELVERTRT GGAEIVNHLK QGSAFYAPAT SVVEMVESIV LDRKRVLTCA
260 270 280 290 300
VSLDGQYGID GTFVGVPVKL GKNGVEHIYE IKLDQSDLDL LQKSAKIVDE
310
NCKMLDASQG
Length:310
Mass (Da):33,092
Last modified:August 30, 2002 - v3
Checksum:i30A92ACFE9442A93
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti227 – 2271A → S in CAA56810. (PubMed:8955383)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80838 Genomic DNA. Translation: CAA56810.1.
AE006470 Genomic DNA. Translation: AAM72734.1.
RefSeqiNP_662392.1. NC_002932.3.
WP_010933173.1. NC_002932.3.

Genome annotation databases

EnsemblBacteriaiAAM72734; AAM72734; CT1507.
GeneIDi1007223.
KEGGicte:CT1507.
PATRICi21400925. VBIChlTep116050_1367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X80838 Genomic DNA. Translation: CAA56810.1 .
AE006470 Genomic DNA. Translation: AAM72734.1 .
RefSeqi NP_662392.1. NC_002932.3.
WP_010933173.1. NC_002932.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GUZ X-ray 2.00 A/B/C/D 1-71 [» ]
1GV0 X-ray 2.50 A/B 1-310 [» ]
ProteinModelPortali P80039.
SMRi P80039. Positions 1-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 194439.CT1507.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM72734 ; AAM72734 ; CT1507 .
GeneIDi 1007223.
KEGGi cte:CT1507.
PATRICi 21400925. VBIChlTep116050_1367.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CTEP194439:GHN0-1546-MONOMER.

Miscellaneous databases

EvolutionaryTracei P80039.

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 mesophile Chlorobium vibrioforme and from the mild thermophile Chlorobium tepidum: molecular cloning, construction of a hybrid, and expression in Escherichia coli."
    Naterstad K., Lauvrak V., Sirevag R.
    J. Bacteriol. 178:7047-7052(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49652 / DSM 12025 / TLS.
  3. "Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, and Heliobacterium gestii: purification, characterization, and investigation of dinucleotide binding by dehydrogenases by use of empirical methods of protein sequence analysis."
    Charnock C.B., Refseth U.H., Strevaag R.
    J. Bacteriol. 174:1307-1313(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-34.
  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 (2.5 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.

Entry informationi

Entry nameiMDH_CHLTE
AccessioniPrimary (citable) accession number: P80039
Secondary accession number(s): P94677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: August 30, 2002
Last modified: October 29, 2014
This is version 122 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