SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q60176

- MDH_METJA

UniProt

Q60176 - MDH_METJA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Malate dehydrogenase
Gene
mdh, mdhB, MJ0490
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reversible oxidation of malate to oxaloacetate. Also catalyzes the reduction of sulfopyruvate, but not pyruvate, nor alpha-ketoglutarate. Higher selectivity for the coenzyme NADPH.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861Substrate By similarity
Binding sitei92 – 921Substrate By similarity
Binding sitei99 – 991NADP
Binding sitei123 – 1231Substrate By similarity
Binding sitei154 – 1541Substrate By similarity
Active sitei178 – 1781Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 137NADPUniRule annotation
Nucleotide bindingi34 – 374NADPUniRule annotation
Nucleotide bindingi121 – 1233NADPUniRule annotation

GO - Molecular functioni

  1. L-lactate dehydrogenase activity Source: InterPro
  2. L-malate dehydrogenase activity Source: UniProtKB-HAMAP
  3. malate dehydrogenase (NADP+) activity Source: UniProtKB-EC

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, NADP

Enzyme and pathway databases

BRENDAi1.1.1.272. 3263.
SABIO-RKQ60176.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37, EC:1.1.1.82)
Gene namesi
Name:mdh
Synonyms:mdhB
Ordered Locus Names:MJ0490
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
ProteomesiUP000000805: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Malate dehydrogenaseUniRule annotation
PRO_0000113485Add
BLAST

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi243232.MJ0490.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Turni7 – 93
Helixi11 – 2111
Beta strandi28 – 336
Helixi35 – 373
Helixi38 – 5215
Beta strandi60 – 656
Helixi69 – 724
Beta strandi76 – 805
Helixi92 – 11322
Beta strandi117 – 1204
Beta strandi122 – 1243
Helixi125 – 13612
Beta strandi142 – 1454
Helixi149 – 16315
Helixi167 – 1693
Beta strandi174 – 1763
Beta strandi182 – 1843
Helixi186 – 1883
Helixi196 – 1983
Helixi200 – 2045
Helixi207 – 21711
Helixi219 – 2224
Beta strandi225 – 2273
Helixi232 – 24413
Beta strandi249 – 26315
Beta strandi265 – 27612
Beta strandi279 – 2835
Helixi290 – 31021

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HYEX-ray1.90A1-313[»]
1HYGX-ray2.80A/B1-313[»]
ProteinModelPortaliQ60176.
SMRiQ60176. Positions 1-313.

Miscellaneous databases

EvolutionaryTraceiQ60176.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.
KOiK00024.
OMAiDSDKDQW.
PhylomeDBiQ60176.

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.
IPR018177. L-lactate_DH_AS.
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.

Sequencei

Sequence statusi: Complete.

Q60176-1 [UniParc]FASTAAdd to Basket

« Hide

MKVTIIGASG RVGSATALLL AKEPFMKDLV LIGREHSINK LEGLREDIYD    50
ALAGTRSDAN IYVESDENLR IIDESDVVII TSGVPRKEGM SRMDLAKTNA 100
KIVGKYAKKI AEICDTKIFV ITNPVDVMTY KALVDSKFER NQVFGLGTHL 150
DSLRFKVAIA KFFGVHIDEV RTRIIGEHGD SMVPLLSATS IGGIPIQKFE 200
RFKELPIDEI IEDVKTKGEQ IIRLKGGSEF GPAAAILNVV RCIVNNEKRL 250
LTLSAYVDGE FDGIRDVCIG VPVKIGRDGI EEVVSIELDK DEIIAFRKSA 300
EIIKKYCEEV KNL 313
Length:313
Mass (Da):34,609
Last modified:November 1, 1997 - v1
Checksum:iA7C0DB67C50151CC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB98481.1.
PIRiB64361.
RefSeqiNP_247466.1. NC_000909.1.
WP_010869991.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98481; AAB98481; MJ_0490.
GeneIDi1451352.
KEGGimja:MJ_0490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L77117 Genomic DNA. Translation: AAB98481.1 .
PIRi B64361.
RefSeqi NP_247466.1. NC_000909.1.
WP_010869991.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HYE X-ray 1.90 A 1-313 [» ]
1HYG X-ray 2.80 A/B 1-313 [» ]
ProteinModelPortali Q60176.
SMRi Q60176. Positions 1-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243232.MJ0490.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB98481 ; AAB98481 ; MJ_0490 .
GeneIDi 1451352.
KEGGi mja:MJ_0490.

Phylogenomic databases

eggNOGi COG0039.
KOi K00024.
OMAi DSDKDQW.
PhylomeDBi Q60176.

Enzyme and pathway databases

BRENDAi 1.1.1.272. 3263.
SABIO-RK Q60176.

Miscellaneous databases

EvolutionaryTracei Q60176.

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.
IPR018177. L-lactate_DH_AS.
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.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea."
    Graupner M., Xu H., White R.H.
    J. Bacteriol. 182:3688-3692(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase."
    Madern D.
    Mol. Microbiol. 37:1515-1520(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Differences in the oligomeric states of the LDH-like L-MalDH from the hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus fulgidus."
    Madern D., Ebel C., Dale H.A., Lien T., Steen I.H., Birkeland N.-K., Zaccai G.
    Biochemistry 40:10310-10316(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  5. "Crystal structure of the MJ0490 gene product of the hyperthermophilic archaebacterium Methanococcus jannaschii, a novel member of the lactate/malate family of dehydrogenases."
    Lee B.I., Chang C., Cho S.-J., Eom S.H., Kim K.K., Yu Y.G., Suh S.W.
    J. Mol. Biol. 307:1351-1362(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

Entry informationi

Entry nameiMDH_METJA
AccessioniPrimary (citable) accession number: Q60176
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 115 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. Methanococcus jannaschii
    Methanococcus jannaschii: 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

External Data

Dasty 3

Similar proteinsi