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 13-SEP-2023, entry version 122. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR01772; MDH_euk_gproteo; 1. DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1. DR PANTHER; PTHR11540:SF58; MALATE DEHYDROGENASE 1, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 //