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Sequence of MDH_METFV

EC Number:1.1.1.37

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
malate dehydrogenase
P16142
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
339
36762
Reaction
(S)-malate + NAD+ = oxaloacetate + NADH + H+
Other sequences found for EC No. 1.1.1.37

EC Number:1.1.1.82

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
malate dehydrogenase (NADP+)
P16142
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
339
36762
Reaction
(S)-malate + NADP+ = oxaloacetate + NADPH + H+
Other sequences found for EC No. 1.1.1.82

EC Number:1.1.1.310

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
(S)-sulfolactate dehydrogenase
P16142
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
339
36762
Reaction
(2S)-3-sulfolactate + NAD+ = 3-sulfopyruvate + NADH + H+
Other sequences found for EC No. 1.1.1.310

EC Number:1.1.1.337

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
L-2-hydroxycarboxylate dehydrogenase (NAD+)
P16142
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
339
36762
Reaction
a (2S)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other sequences found for EC No. 1.1.1.337

General information:

Sequence
  0 MIISPEEERS LIIKILNALG VSEEHAKITA DVIVDADLKG FTSHGIGRFP QYVEGIKLGT
 60 IKTSGNIEIE KETDSVALIN GNHLLGQVVA YKGMKLAIEK AKNTGVGIVG IHDSNHFGIA
120 GYYSDMAMKN DMIGITMTNT EPAVAPLGGK IPVLGTNPIA ISIPSNEYYV AVDMSTAAVA
180 RGKLLEAARK NEKIPEGIAV DKNGNPTTDP NEALNGSILP FGGHKGYALC FMIEILAGPL
240 VKAEFGSKVK GTVDPSQMCT KGDLLIAIDP SKFYDIEEFK RNVDEFVKEI KSTGKDVLIP
300 GDRERMNIKK REKEGIELDK KLVEKLKEIA DELNIELTW
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
57660
Honka E.,Fabry S.,Niermann T.,Palm P.,Hensel R.
Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus.
Eur. J. Biochem.
188
623-632
1990
57661
Anderson I.,Djao O.D.,Misra M.,Chertkov O.,Nolan M.,Lucas S.,Lapidus A.,Del Rio T.G.,Tice H.,Cheng J.F.,Tapia R.,Han C.,Goodwin L.,Pitluck S.,Liolios K.,Ivanova N.,Mavromatis K.,Mikhailova N.,Pati A.,Brambilla E.,Chen A.,Palaniappan K.,Land M.,Hauser L.,Chang Y.J.,Jeffries C.D.,Sikorski J.,Spring S.,Rohde M.,Eichinger K.,Huber H.,Wirth R.,Goker M.,Detter J.C.,Woyke T.,Bristow J.,Eisen J.A.,Markowitz V.,Hugenholtz P.,Klenk H.P.,Kyrpides N.C.
Complete genome sequence of Methanothermus fervidus type strain (V24S).
Stand. Genomic Sci.
3
315-324
2010
57662
Graupner M.,Xu H.,White R.H.
Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.
J. Bacteriol.
182
3688-3692
2000