MDHG_CITLA
ID MDHG_CITLA Reviewed; 356 AA.
AC P19446;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Malate dehydrogenase, glyoxysomal;
DE EC=1.1.1.37;
DE Flags: Precursor;
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;
RX PubMed=2377615; DOI=10.1073/pnas.87.15.5773;
RA Gietl C.;
RT "Glyoxysomal malate dehydrogenase from watermelon is synthesized with an
RT amino-terminal transit peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5773-5777(1990).
RN [2]
RP PROTEIN SEQUENCE OF 37-65.
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 N-TERMINUS, X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN
RP COMPLEX WITH SUBSTRATE ANALOG, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15670147; DOI=10.1111/j.1742-4658.2004.04475.x;
RA Cox B., Chit M.M., Weaver T., Gietl C., Bailey J., Bell E., Banaszak L.;
RT "Organelle and translocatable forms of glyoxysomal malate dehydrogenase.
RT The effect of the N-terminal presequence.";
RL FEBS J. 272:643-654(2005).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=146 uM for NADH;
CC KM=76 mM for oxaloacetate;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15670147}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome.
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; M33148; AAA33041.1; -; mRNA.
DR PIR; A35957; DEPUGW.
DR PDB; 1SEV; X-ray; 2.55 A; A/B=1-356.
DR PDB; 1SMK; X-ray; 2.50 A; A/B/C/D/E/F/G/H=37-356.
DR PDBsum; 1SEV; -.
DR PDBsum; 1SMK; -.
DR AlphaFoldDB; P19446; -.
DR SMR; P19446; -.
DR PRIDE; P19446; -.
DR EnsemblPlants; Cla97C01G017230.1; Cla97C01G017230.1; Cla97C01G017230.
DR Gramene; Cla97C01G017230.1; Cla97C01G017230.1; Cla97C01G017230.
DR EvolutionaryTrace; P19446; -.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
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 3D-structure; Direct protein sequencing; Glyoxylate bypass; Glyoxysome;
KW NAD; Oxidoreductase; Peroxisome; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..36
FT /note="Glyoxysome"
FT /evidence="ECO:0000269|PubMed:15670147, ECO:0000269|Ref.2"
FT CHAIN 37..356
FT /note="Malate dehydrogenase, glyoxysomal"
FT /id="PRO_0000018638"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT BINDING 51..57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="substrate"
FT BINDING 130
FT /ligand="substrate"
FT BINDING 137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 160..162
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT BINDING 196
FT /ligand="substrate"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 132..151
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 240..260
FT /evidence="ECO:0007829|PDB:1SMK"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 269..287
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 302..315
FT /evidence="ECO:0007829|PDB:1SMK"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:1SMK"
FT HELIX 330..354
FT /evidence="ECO:0007829|PDB:1SMK"
SQ SEQUENCE 356 AA; 37637 MW; 4B0C8101DC11FC7F CRC64;
MQPIPDVNQR IARISAHLHP PKSQMEESSA LRRANCRAKG GAPGFKVAIL GAAGGIGQPL
AMLMKMNPLV SVLHLYDVVN APGVTADISH MDTGAVVRGF LGQQQLEAAL TGMDLIIVPA
GVPRKPGMTR DDLFKINAGI VKTLCEGIAK CCPRAIVNLI SNPVNSTVPI AAEVFKKAGT
YDPKRLLGVT MLDVVRANTF VAEVLGLDPR DVDVPVVGGH AGVTILPLLS QVKPPSSFTQ
EEISYLTDRI QNGGTEVVEA KAGAGSATLS MAYAAVKFAD ACLRGLRGDA GVIECAFVSS
QVTELPFFAS KVRLGRNGIE EVYSLGPLNE YERIGLEKAK KELAGSIEKG VSFIRS
