MDHM_FRAAN
ID MDHM_FRAAN Reviewed; 339 AA.
AC P83373;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Malate dehydrogenase, mitochondrial;
DE EC=1.1.1.37;
DE Flags: Precursor;
GN Name=MMDHI;
OS Fragaria ananassa (Strawberry) (Fragaria chiloensis x Fragaria virginiana).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Potentilleae; Fragariinae;
OC Fragaria.
OX NCBI_TaxID=3747 {ECO:0000305};
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 20-37.
RC STRAIN=cv. Elsanta; TISSUE=Fruit;
RX PubMed=15086813; DOI=10.1111/j.0031-9317.2004.00302.x;
RA Iannetta P.P.M., Escobar N.M., Ross H.A., Souleyre E.J., Hancock R.D.,
RA Witte C.P., Davies H.V.;
RT "Identification, cloning and expression analysis of strawberry (Fragaria x
RT ananassa) mitochondrial citrate synthase and mitochondrial malate
RT dehydrogenase.";
RL Physiol. Plantarum 121:15-26(2004).
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, ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000305}.
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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 Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:15086813"
FT CHAIN 20..339
FT /note="Malate dehydrogenase, mitochondrial"
FT /id="PRO_0000018627"
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 33..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 142..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 339 AA; 35622 MW; 22D4EF65E225A00C CRC64;
MRPSMSLIRS VSRVARRGYS SESVPQRKVA VLGAAGGIGQ PLALLMKLNP LVSQLSLYDI
AGTPGVAADV SHINTRSEVK GYAGEEQLGE ALEGCDVVII PAGVPRKPGM TRDDLFNINA
GIVRSLTAAI AKYCPHAIIN MISNPVNSTV PIASEVLKKA GVYDEKKLFG VTTLDVVRAK
TFYAGKAGVP VAEVNVPVVG GHAGITILPL FSQATPKANL SDDYIKALTK RTQDGGTEVV
EAKAGKGSAT LSMAYAGALF ADACLXGLNG VPDVVECSYV QSSITELPFF ASKVRLGKNG
VEEVLDLGPL SDFEKEGLKQ LKPELKSSIE KGIKFANQS