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MDHP_MAIZE
ID   MDHP_MAIZE              Reviewed;         432 AA.
AC   P15719;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE            EC=1.1.1.82;
DE   AltName: Full=NADP-MDH;
DE   Flags: Precursor;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Metzler M., Rothermel B.A., Nelson T.;
RT   "Maize NADP-malate dehydrogenase: cDNA cloning, sequence, and mRNA
RT   characterization.";
RL   Plant Mol. Biol. 12:713-722(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 58-84.
RX   PubMed=3403553; DOI=10.1016/s0021-9258(18)37852-9;
RA   Decottignies P., Schmitter J.-M., Miginiac-Maslow M., le Marechal P.,
RA   Jacquot J.-P., Gadal P.;
RT   "Primary structure of the light-dependent regulatory site of corn NADP-
RT   malate dehydrogenase.";
RL   J. Biol. Chem. 263:11780-11785(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 41-62.
RX   PubMed=16668822; DOI=10.1104/pp.98.4.1506;
RA   Agostino A., Jeffrey P., Hatch M.D.;
RT   "Amino acid sequence and molecular weight of native NADP malate
RT   dehydrogenase from the C4 plant Zea mays.";
RL   Plant Physiol. 98:1506-1510(1992).
CC   -!- FUNCTION: The chloroplastic, NADP-dependent form is essential for the
CC       photosynthesis C4 cycle, which allows plants to circumvent the problem
CC       of photorespiration. In C4 plants, NADP-MDH activity acts to convert
CC       oxaloacetate to malate in chloroplasts of mesophyll cells for transport
CC       to the bundle sheath cells.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate;
CC         Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82;
CC   -!- ACTIVITY REGULATION: Chloroplast NADP-MDH is activated upon
CC       illumination. In order to be enzymatically active, disulfide bridges on
CC       the protein must be reduced by thioredoxin which receives electrons
CC       from ferredoxin and the electron transport system of photosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X16084; CAA34213.1; -; mRNA.
DR   PIR; S04859; DEMZMC.
DR   RefSeq; NP_001105420.1; NM_001111950.1.
DR   AlphaFoldDB; P15719; -.
DR   SMR; P15719; -.
DR   STRING; 4577.GRMZM2G129513_P01; -.
DR   PaxDb; P15719; -.
DR   PRIDE; P15719; -.
DR   GeneID; 542374; -.
DR   MaizeGDB; 40092; -.
DR   eggNOG; KOG1496; Eukaryota.
DR   OrthoDB; 1118998at2759; -.
DR   BRENDA; 1.1.1.82; 6752.
DR   SABIO-RK; P15719; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P15719; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.90.110.10; -; 1.
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; IPR011273; Malate_DH_NADP-dep_pln.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01757; Malate-DH_plant; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Disulfide bond; NADP;
KW   Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:16668822"
FT   CHAIN           41..432
FT                   /note="Malate dehydrogenase [NADP], chloroplastic"
FT                   /id="PRO_0000018643"
FT   REGION          18..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         96..102
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         190
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         214..216
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   SITE            67
FT                   /note="Activation of NADP-MDH"
FT   SITE            72
FT                   /note="Activation of NADP-MDH"
FT   DISULFID        67..72
FT                   /note="In oxidized inactive NAD-MDH"
FT                   /evidence="ECO:0000269|PubMed:3403553"
FT   DISULFID        408..420
FT                   /note="In oxidized inactive NAD-MDH"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  46860 MW;  45531DEF8BBF79FD CRC64;
     MGLSTVYSPA GPRLVPAPLG RCRSAQPRRP RRAPLATVRC SVDATKQAQD GVATAVATEA
     PASRKECFGV FCTTYDLKAE DKTKSWRKLV NVAVSGAAGM ISNHLLFKLA SGEVFGQDQP
     IALKLLGSER SFQALEGVAM ELEDSLYPLL REVSIGIDPY VVFQDVDWAL LIGAKPRGPG
     MERAALLDIN GQIFADQGKA LNAVASRNDE VLVVGNPCNT NALICLKNAP NIPAKNFHAL
     TRLDENRAKC QLALKAGVFY DKVSNVTIWG NHSTTQVPDF LNAKIDGRPV KEVIKDTKWL
     EEEFTLTVQK RGGVLIQKWG RSSAASTAVS IVDAIRSLVT PTPEGDWFST GVYTTGNPYG
     IAEDIVFSMP CRSKGDGDYE LASDVLMDDF LWERIKKSEA ELLAEKKCVA HLTGEGNAFC
     DLPEDTMLPG EV
 
 
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