ID E3V1Z6_PINSY Unreviewed; 278 AA.
AC E3V1Z6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU003405};
DE Flags: Fragment;
GN Name=mdhA {ECO:0000313|EMBL:ADP03225.1};
OS Pinus sylvestris (Scotch pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=3349 {ECO:0000313|EMBL:ADP03225.1};
RN [1] {ECO:0000313|EMBL:ADP03225.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Uusikaupunki 173 {ECO:0000313|EMBL:ADP03243.1}, Uusikaupunki
RC 261 {ECO:0000313|EMBL:ADP03246.1}, Uusikaupunki 33
RC {ECO:0000313|EMBL:ADP03225.1}, and Uusikaupunki 364
RC {ECO:0000313|EMBL:ADP03253.1};
RA Pyhajarvi T., Kujala S.T., Savolainen O.;
RT "Revisiting protein heterozygosity in plants-nucleotide diversity in
RT allozyme coding genes of conifer Pinus sylvestris.";
RL Tree Genet. Genomes 0:0-0(2010).
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:0000256|RuleBase:RU003405};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613}.
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DR EMBL; HM853199; ADP03225.1; -; Genomic_DNA.
DR EMBL; HM853217; ADP03243.1; -; Genomic_DNA.
DR EMBL; HM853220; ADP03246.1; -; Genomic_DNA.
DR EMBL; HM853227; ADP03253.1; -; Genomic_DNA.
DR AlphaFoldDB; E3V1Z6; -.
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 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; IPR011274; Malate_DH_NAD-dep_euk.
DR InterPro; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR NCBIfam; TIGR01758; MDH_euk_cyt; 1.
DR PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR23382:SF3; MALATE DEHYDROGENASE, CYTOPLASMIC; 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 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU003405};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT DOMAIN 2..99
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 103..271
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 76..78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADP03225.1"
SQ SEQUENCE 278 AA; 29942 MW; FE383C76280F0E3E CRC64;
KMELIDAAFP LLKGIVATTD PVEACSGVNI AVMVGGFPRK EGMERKDVMS KNVSIYKSQA
SALEQHAAPN CKVLVVANPA NTNALILKEF APSIPEKNVT CLTRLDHNRA LGQISERLHV
PVSNVKNVII WGNHSSSQYP DVYHASVVTG AGEKPVRELV ADDAWLDGEF ITTVQQRGAA
IIKARKLSSA LSAASSACDH IRDWVLGTPK GTFVSMGVYS DGSYDVPPGI IFSYPVTCEN
GSWSIVQGLP INEFSRKKLD ATANELVEEK ALAYSCLT
//
