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O08349

- MDH_ARCFU

UniProt

O08349 - MDH_ARCFU

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Protein
Malate dehydrogenase
Gene
mdh, AF_0855
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 5 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 sitei32 – 321NAD
Binding sitei81 – 811Substrate By similarity
Binding sitei87 – 871Substrate By similarity
Binding sitei94 – 941NAD
Binding sitei119 – 1191Substrate By similarity
Binding sitei150 – 1501Substrate By similarity
Active sitei172 – 1721Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 126NADUniRule annotation
Nucleotide bindingi117 – 1193NADUniRule annotation

GO - Molecular functioni

  1. L-lactate dehydrogenase activity Source: InterPro
  2. L-malate dehydrogenase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciAFUL224325:GJBC-873-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase (EC:1.1.1.37)
Gene namesi
Name:mdh
Ordered Locus Names:AF_0855
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199: 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 – 294294Malate dehydrogenaseUniRule annotation
PRO_0000113480Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224325.AF0855.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Helixi10 – 2213
Beta strandi26 – 316
Helixi35 – 4915
Helixi50 – 523
Beta strandi57 – 626
Helixi64 – 674
Beta strandi71 – 755
Beta strandi83 – 853
Helixi87 – 10620
Beta strandi113 – 1164
Beta strandi118 – 1203
Helixi121 – 13111
Beta strandi138 – 1414
Helixi144 – 15714
Beta strandi161 – 1633
Beta strandi168 – 1703
Helixi180 – 1823
Beta strandi185 – 1873
Helixi191 – 1999
Helixi201 – 2099
Helixi214 – 22815
Beta strandi234 – 24310
Helixi244 – 2463
Beta strandi248 – 25912
Beta strandi262 – 2654
Helixi272 – 29019
Turni291 – 2933

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X0IX-ray2.90A1-294[»]
2X0JX-ray2.79A1-294[»]
ProteinModelPortaliO08349.
SMRiO08349. Positions 1-294.

Miscellaneous databases

EvolutionaryTraceiO08349.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0039.
KOiK00024.
OMAiYAPSAFV.

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.

O08349-1 [UniParc]FASTAAdd to Basket

« Hide

MKLGFVGAGR VGSTSAFTCL LNLDVDEIAL VDIAEDLAVG EAMDLAHAAA    50
GIDKYPKIVG GADYSLLKGS EIIVVTAGLA RKPGMTRLDL AHKNAGIIKD 100
IAKKIVENAP ESKILVVTNP MDVMTYIMWK ESGKPRNEVF GMGNQLDSQR 150
LKERLYNAGA RNIRRAWIIG EHGDSMFVAK SLADFDGEVD WEAVENDVRF 200
VAAEVIKRKG ATIFGPAVAI YRMVKAVVED TGEIIPTSMI LQGEYGIENV 250
AVGVPAKLGK NGAEVADIKL SDEEIEKLRN SAKILRERLE ELGY 294
Length:294
Mass (Da):31,874
Last modified:July 1, 1997 - v1
Checksum:i90389DBC189B944F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z85985 Genomic DNA. Translation: CAB06654.1.
AE000782 Genomic DNA. Translation: AAB90384.1.
PIRiG69356.
RefSeqiNP_069689.1. NC_000917.1.
WP_010878358.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90384; AAB90384; AF_0855.
GeneIDi1484074.
KEGGiafu:AF0855.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z85985 Genomic DNA. Translation: CAB06654.1 .
AE000782 Genomic DNA. Translation: AAB90384.1 .
PIRi G69356.
RefSeqi NP_069689.1. NC_000917.1.
WP_010878358.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2X0I X-ray 2.90 A 1-294 [» ]
2X0J X-ray 2.79 A 1-294 [» ]
ProteinModelPortali O08349.
SMRi O08349. Positions 1-294.
ModBasei Search...

Protein-protein interaction databases

STRINGi 224325.AF0855.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB90384 ; AAB90384 ; AF_0855 .
GeneIDi 1484074.
KEGGi afu:AF0855.

Phylogenomic databases

eggNOGi COG0039.
KOi K00024.
OMAi YAPSAFV.

Enzyme and pathway databases

BioCyci AFUL224325:GJBC-873-MONOMER.

Miscellaneous databases

EvolutionaryTracei O08349.

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. "Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus."
    Langelandsvik A.S., Steen I.H., Birkeland N.K., Lien T.
    Arch. Microbiol. 168:59-67(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  3. "The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation."
    Irimia A., Vellieux F.M.D., Madern D., Zaccai G., Karshikoff A., Tibbelin G., Ladenstein R., Lien T., Birkeland N.-K.
    J. Mol. Biol. 335:343-356(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.

Entry informationi

Entry nameiMDH_ARCFU
AccessioniPrimary (citable) accession number: O08349
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 119 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. 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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