Sequence of MDH_HALMA
EC Number:1.1.1.37
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
malate dehydrogenase
Q07841
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
304
32808
Reaction
(S)-malate + NAD+ = oxaloacetate + NADH + H+
Other sequences found for EC No. 1.1.1.37
General information:
Sequence
0 MTKVSVVGAA GTVGAAAGYN IALRDIADEV VFVDIPDKED DTVGQAADTN HGIAYDSNTR
60 VRQGGYEDTA GSDVVVITAG IPRQPGQTRI DLAGDNAPIM EDIQSSLDEH NDDYISLTTS
120 NPVDLLNRHL YEAGDRSREQ VIGFGGRLDS ARFRYVLSEE FDAPVQNVEG TILGEHGDAQ
180 VPVFSKVRVD GTDPEFSGDE KEQLLGDLQE SAMDVIERKG ATEWGPARGV AHMVEAILHD
240 TGEVLPASVK LEGEFGHEDT AFGVPVRLGS NGVEEIVEWD LDDYEQDLMA DAAEKLSDQY
300 DKIS
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
441264
Cendrin F.,Chroboczek J.,Zaccai G.,Eisenberg H.,Mevarech M.
Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui.
Biochemistry
32
4308-4313
1993
441265
Baliga N.S.,Bonneau R.,Facciotti M.T.,Pan M.,Glusman G.,Deutsch E.W.,Shannon P.,Chiu Y.,Weng R.S.,Gan R.R.,Hung P.,Date S.V.,Marcotte E.,Hood L.,Ng W.V.
Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.
Genome Res.
14
2221-2234
2004
441266
Madern D.,Ebel C.,Mevarech M.,Richard S.B.,Pfister C.,Zaccai G.
Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui.
Biochemistry
39
1001-1010
2000
441268
Richard S.B.,Madern D.,Garcin E.,Zaccai G.
Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui.
Biochemistry
39
992-1000
2000
441269
Irimia A.,Ebel C.,Madern D.,Richard S.B.,Cosenza L.W.,Zaccai G.,Vellieux F.M.D.
The oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies.
J. Mol. Biol.
326
859-873
2003
