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MAOC_ORYSJ
ID   MAOC_ORYSJ              Reviewed;         639 AA.
AC   P43279; Q0JQ07; Q9LDH7;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=NADP-dependent malic enzyme, chloroplastic;
DE            Short=NADP-ME;
DE            EC=1.1.1.40;
DE   Flags: Precursor;
GN   Name=ME6; OrderedLocusNames=Os01g0188400, LOC_Os01g09320;
GN   ORFNames=OsJ_00690 {ECO:0000312|EMBL:EEE54023.1}, P0512G09.20, P0695A04.29;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Callus;
RX   PubMed=8204833; DOI=10.1007/bf00014450;
RA   Fushimi T., Umeda M., Shimazaki T., Kato A., Toriyama K., Uchimiya H.;
RT   "Nucleotide sequence of a rice cDNA similar to a maize NADP-dependent malic
RT   enzyme.";
RL   Plant Mol. Biol. 24:965-967(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: The chloroplastic ME isoform decarboxylates malate shuttled
CC       from neighboring mesophyll cells. The CO(2) released is then refixed by
CC       ribulose-bisphosphate carboxylase. This pathway eliminates the
CC       photorespiratory loss of CO(2) that occurs in most plants.
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   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; D16499; BAA03949.1; -; mRNA.
DR   EMBL; AP002816; BAB03427.1; -; Genomic_DNA.
DR   EMBL; AP002836; BAB07934.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF04171.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS70801.1; -; Genomic_DNA.
DR   EMBL; CM000138; EEE54023.1; -; Genomic_DNA.
DR   EMBL; AK121770; BAH00649.1; -; mRNA.
DR   PIR; S46499; S46499.
DR   RefSeq; XP_015621553.1; XM_015766067.1.
DR   AlphaFoldDB; P43279; -.
DR   SMR; P43279; -.
DR   STRING; 4530.OS01T0188400-01; -.
DR   PaxDb; P43279; -.
DR   PRIDE; P43279; -.
DR   EnsemblPlants; Os01t0188400-01; Os01t0188400-01; Os01g0188400.
DR   GeneID; 4326769; -.
DR   Gramene; Os01t0188400-01; Os01t0188400-01; Os01g0188400.
DR   KEGG; osa:4326769; -.
DR   eggNOG; KOG1257; Eukaryota.
DR   HOGENOM; CLU_011405_5_2_1; -.
DR   InParanoid; P43279; -.
DR   OMA; GDACLQY; -.
DR   OrthoDB; 435571at2759; -.
DR   SABIO-RK; P43279; -.
DR   UniPathway; UPA00322; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; P43279; baseline and differential.
DR   Genevisible; P43279; OS.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0004470; F:malic enzyme activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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   Chloroplast; Metal-binding; NAD; NADP; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..639
FT                   /note="NADP-dependent malic enzyme, chloroplastic"
FT                   /id="PRO_0000018548"
FT   REGION          15..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        258
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         383..399
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         495
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            354
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        45
FT                   /note="Missing (in Ref. 1; BAA03949)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50..52
FT                   /note="AAA -> TPV (in Ref. 1; BAA03949)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="S -> A (in Ref. 1; BAA03949)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        602
FT                   /note="S -> T (in Ref. 1; BAA03949)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   639 AA;  69866 MW;  A12C763D31D8D25D CRC64;
     MLSARAAATA AAAAASPLWK RGEGGSSGSG SGCTSCREVR RRAAAVRVRA AAPRRVEAVA
     MESAAETEKK EEVAAAGGGV EDMATEEVPV TPWAFSVASG YTLLRDPHHN KGLAFSEKER
     DAHYLRGLLP PAVVSQDLQV KKIMHNLRQY SVPLQRYMAM MDLQERNERL FYKLLIDNVE
     ELLPVVYTPT VGEACQKYGS IFRQPQGLYV SLKDKGKVLD VLRNWPERNI QVIVVTDGER
     ILGLGDLGCQ GMGIPVGKLS LYTALGGVRP SACLPITIDV GTNNEQLLND EFYIGLRQRR
     ATGKEYHELM EEFMSAVKQI YGEKVLIQFE DFANHNAFDL LAKYSKSHLV FNDDIQGTAS
     VVLAGLLSSL KVVGGTLAEH TYLFLGAGEA GTGIAELIAL EISKQTKAPI EECRKKVWLL
     DSKGLIVNSR KESLQAFKKP WAHEHEPVTT LLDAVQSIKP TVLIGTSGVG KTFTKEVIEA
     MASFNERPVI FSLSNPTSHS ECTAEEAYNW SQGRAVFASG SPFDPVEYNG KIHVPGQSNN
     AYIFPGFGLG VVISGAVRVH EDMLLAASET LADQATQENF EKGSIFPPFT NIRKISARIA
     ASVAAKAYEL GLATRLPQPR DLEKYAESCM YTPVYRSYR
 
 
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