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MDHP_MEDSA
ID   MDHP_MEDSA              Reviewed;         437 AA.
AC   O48902;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Malate dehydrogenase [NADP], chloroplastic;
DE            EC=1.1.1.82;
DE   AltName: Full=NADP-MDH;
DE   Flags: Precursor;
GN   Name=MDH1; Synonyms=P1MDH;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Saranac; TISSUE=Root nodule;
RX   PubMed=9721676; DOI=10.1046/j.1365-313x.1998.00192.x;
RA   Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P.;
RT   "Alfalfa malate dehydrogenase (MDH): molecular cloning and characterization
RT   of five different forms reveals a unique nodule-enhanced MDH.";
RL   Plant J. 15:173-184(1998).
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 (By similarity). {ECO:0000250}.
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, disulfides bridges
CC       on the protein must be reduced by thioredoxin which receives electrons
CC       from ferredoxin and the electron transport system of photosynthesis (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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; AF020269; AAB99753.1; -; mRNA.
DR   AlphaFoldDB; O48902; -.
DR   SMR; O48902; -.
DR   PRIDE; O48902; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0046554; F:malate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; NADP; Oxidoreductase; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..437
FT                   /note="Malate dehydrogenase [NADP], chloroplastic"
FT                   /id="PRO_0000018644"
FT   ACT_SITE        277
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         101..107
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         195
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..221
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10004"
FT   SITE            72
FT                   /note="Activation of NADP-MDH"
FT                   /evidence="ECO:0000250"
FT   SITE            77
FT                   /note="Activation of NADP-MDH"
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..77
FT                   /note="In oxidized inactive NAD-MDH"
FT                   /evidence="ECO:0000250"
FT   DISULFID        413..425
FT                   /note="In oxidized inactive NAD-MDH"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   437 AA;  47835 MW;  9C7C5377DBA5454A CRC64;
     MALTQLNNTC SKTQLHSSSQ LSFLSRTLPR HHHCTLAPLH RTQHARISCS VAPNQVQAPA
     VQTQDPKSKP DCYGVFCLTY DLKAEEETKS WKKLITIAVS GAAGMISNHL LFKLASGEVF
     GPNQPIALKL LGSERSLQAL EGVAMELEDS LFPLLREVVI SIDPYEVFQD AEWALLIGAK
     PRGPGMERAA LLDINGQIFA EQGKALNAVA SRNVKVIVVG NPCNTNALIC LKNAPNIPAK
     NFHALTRLDE NRAKCQLALK AGVFYDKVSN MTIWGNHSTT QVPDFLNARI DGLPVKEVIK
     DHKWLEEEFT EKVQKRGGAL IQKWGRSSAA STSVSIVDAI RSLIIPTPEG DWFSTGVYTT
     GNPYGIAEDI VFSMPCRSKG DGDYELVKDV IFDDYLRQKL AKTEAELLAE KKCVAHLTGE
     GIAVCDLPGD TMLPGEM
 
 
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