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MAOX_PHAVU
ID   MAOX_PHAVU              Reviewed;         589 AA.
AC   P12628;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=NADP-dependent malic enzyme;
DE            Short=NADP-ME;
DE            EC=1.1.1.40;
GN   Name=ME1;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3041415; DOI=10.1073/pnas.85.15.5546;
RA   Walter M.H., Grima-Pettenati J., Grand C., Boudet A.M., Lamb C.J.;
RT   "Cinnamyl-alcohol dehydrogenase, a molecular marker specific for lignin
RT   synthesis: cDNA cloning and mRNA induction by fungal elicitor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5546-5550(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Processor; TISSUE=Leaf;
RX   PubMed=7925425; DOI=10.1111/j.1432-1033.1994.t01-1-00999.x;
RA   Walter M.H., Grima-Pettenati J., Feuillet C.;
RT   "Characterization of a bean (Phaseolus vulgaris L.) malic-enzyme gene.";
RL   Eur. J. Biochem. 224:999-1009(1994).
RN   [3]
RP   SIMILARITY TO MALIC ENZYMES.
RX   PubMed=2103472; DOI=10.1007/bf00019173;
RA   Walter M.H., Grima-Pettenati J., Grand C., Boudet A.M., Lamb C.J.;
RT   "Extensive sequence similarity of the bean CAD4 (cinnamyl-alcohol
RT   dehydrogenase) to a maize malic enzyme.";
RL   Plant Mol. Biol. 15:525-526(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate;
CC         Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxaloacetate = CO2 + pyruvate; Xref=Rhea:RHEA:15641,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:16526; EC=1.1.1.40;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By fungal elicitor.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a cinnamyl-alcohol dehydrogenase.
CC       {ECO:0000305|PubMed:3041415}.
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DR   EMBL; J03825; AAA19575.1; -; mRNA.
DR   EMBL; X80051; CAA56354.1; -; Genomic_DNA.
DR   PIR; S48198; DEFBC.
DR   AlphaFoldDB; P12628; -.
DR   SMR; P12628; -.
DR   STRING; 3885.XP_007137243.1; -.
DR   PRIDE; P12628; -.
DR   ProMEX; P12628; -.
DR   eggNOG; KOG1257; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; NADP; Oxidoreductase.
FT   CHAIN           1..589
FT                   /note="NADP-dependent malic enzyme"
FT                   /id="PRO_0000160201"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         333..349
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         445
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            304
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        16
FT                   /note="K -> N (in Ref. 2; CAA56354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="A -> E (in Ref. 2; CAA56354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258..259
FT                   /note="TF -> EL (in Ref. 2; CAA56354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="V -> L (in Ref. 2; CAA56354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        567
FT                   /note="K -> P (in Ref. 2; CAA56354)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   589 AA;  64932 MW;  9BFADDB2699BAC1E CRC64;
     MSSISLKENG GEVSVKKDYS NGGGVRDLYG EDSATEDHLI TPWTFSVASG CSLLRDPRYN
     KGLAFTEGER DAHYLRGLLP PSVFNQELQE KRLMHNLRQY EVPLHRYMAL MDLQERNERL
     FYKLLIDNVA ELLPVVYTPT VGEACQKYGS IFRRPQGLYI SLKEKGKILE VLKNWPEKSI
     QVIVVTDGER ILGLGDLGCQ GMGIPVGKLS LYTALGGVRP SSCLPVTIDV GTNNEKLLND
     EFYIGLRQRR ATGQEYATFL DEFMRAVKQN YGEKVLVQFE DFANHNAFDL LEKYSSSHLV
     FNDDIQGTAS VVLAGLLASL KLVGGTLADH TFLFLGAGEA GTGIAELIAV EVSKQTKAPV
     EETRKKIWLV DSKGLIVSSR LESLQQFKKP WAHEHEPVKG LLEAVKAIKP TVLIGSSGAG
     KTFTKEVVET MASLNEKPLI LALSNPTSQS ECTAEEAYTW SKGRAIFASG SPFDPVEYEG
     KLFVPGQANN AYIFPGFGLG LIMSGAIRVR DEMLLAASEA LAAQVSEENY DKGLIYPPFT
     NIRKISANIA AKVAAKAYDL GLASHLKRPK DLVKYAESCM YSPGYRSYR
 
 
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