MDH_PHEIM
ID MDH_PHEIM Reviewed; 25 AA.
AC P19980;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
DE Flags: Fragment;
GN Name=mdh;
OS Phenylobacterium immobile.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=21;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=E;
RX PubMed=2775496; DOI=10.1515/bchm3.1989.370.2.763;
RA Rommel T.O., Hund H.-K., Speth A.R., Lingens F.;
RT "Purification and N-terminal amino-acid sequences of bacterial malate
RT dehydrogenases from six actinomycetales strains and from Phenylobacterium
RT immobile, strain E.";
RL Biol. Chem. Hoppe-Seyler 370:763-768(1989).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10004};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000305}.
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DR PIR; S07574; S07574.
DR AlphaFoldDB; P19980; -.
DR SMR; P19980; -.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..>25
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113385"
FT BINDING 11..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT NON_TER 25
SQ SEQUENCE 25 AA; 2626 MW; C8D81E008825845C CRC64;
SKTPIRVAVT GAAGNIGYHL LFRIA