MDHM_CITLA
ID MDHM_CITLA Reviewed; 347 AA.
AC P17783;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Malate dehydrogenase, mitochondrial;
DE EC=1.1.1.37;
DE AltName: Allergen=Citr l MDH {ECO:0000305};
DE Flags: Precursor;
GN Name=MMDH;
OS Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Citrullus.
OX NCBI_TaxID=3654;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Sugar Baby; TISSUE=Cotyledon;
RX PubMed=2102869; DOI=10.1007/bf00019398;
RA Gietl C., Lehnerer M., Olsen O.;
RT "Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA
RT clones and primary structure of the higher-plant precursor protein.";
RL Plant Mol. Biol. 14:1019-1030(1990).
RN [2]
RP PROTEIN SEQUENCE OF 28-55.
RA Gietl C., Lottspeich F., Hock B.;
RT "Sequence homologies between glyoxysomal and mitochondrial malate
RT dehydrogenase.";
RL Planta 169:555-558(1986).
RN [3]
RP PROTEIN SEQUENCE OF 28-34, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ALLERGEN.
RX PubMed=19295232; DOI=10.1159/000205574;
RA Pastor C., Cuesta-Herranz J., Cases B., Perez-Gordo M., Figueredo E.,
RA de las Heras M., Vivanco F.;
RT "Identification of major allergens in watermelon.";
RL Int. Arch. Allergy Immunol. 149:291-298(2009).
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE in 96% of
CC the 23 patients tested with oral allergy symptoms and pollen allergy to
CC watermelon. IgE-binding is lost by digestion with pepsin.
CC {ECO:0000269|PubMed:19295232}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
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DR EMBL; X17362; CAA35239.1; -; mRNA.
DR PIR; S10162; DEPUMW.
DR AlphaFoldDB; P17783; -.
DR SMR; P17783; -.
DR Allergome; 6159; Citr l MDH.
DR EnsemblPlants; Cla97C07G136660.1; Cla97C07G136660.1; Cla97C07G136660.
DR Gramene; Cla97C07G136660.1; Cla97C07G136660.1; Cla97C07G136660.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR001557; L-lactate/malate_DH.
DR InterPro; IPR022383; Lactate/malate_DH_C.
DR InterPro; IPR001236; Lactate/malate_DH_N.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000305|PubMed:19295232, ECO:0000305|Ref.2"
FT CHAIN 28..347
FT /note="Malate dehydrogenase, mitochondrial"
FT /evidence="ECO:0000305|PubMed:19295232, ECO:0000305|Ref.2"
FT /id="PRO_0000018625"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 41..47
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 36201 MW; 31474F15018D30CC CRC64;
MKASILRSVR SAVSRSSSSN RLLSRSFATE SVPERKVAVL GAAGGIGQPL ALLMKLNPLV
SKLALYDIAG TPGVAADVGH VNTRSEVTGY VGEEQLGKAL EGSDVVIIPA GVPRKPGMTR
DDLFNINAGI VKSLCTAIAK YCPNALINMI SNPVNSTVPI AAEVFKKAGT YDEKKLFGVT
TLDVVRAKTF YAGKANVPVA EVNVPVIGGH AGITILPLFS QATPRANLSD DTIVALTKRT
QDGGTEVVEA KAGKGSATLS MAYAGALFAD ACLKGLNGVP DVVECSFVQS TVTELPFFAS
KVKLGKNGVE SVLDLGPLSD FEKEGLEKLK PELKASIEKG IQFANAN
