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MAOP3_ARATH
ID   MAOP3_ARATH             Reviewed;         588 AA.
AC   Q9XGZ0;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=NADP-dependent malic enzyme 3;
DE            Short=AtNADP-ME3;
DE            Short=NADP-malic enzyme 3;
DE            EC=1.1.1.40;
GN   Name=NADP-ME3; OrderedLocusNames=At5g25880; ORFNames=T1N24.25;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=16113210; DOI=10.1104/pp.105.065953;
RA   Wheeler M.C., Tronconi M.A., Drincovich M.F., Andreo C.S., Fluegge U.-I.,
RA   Maurino V.G.;
RT   "A comprehensive analysis of the NADP-malic enzyme gene family of
RT   Arabidopsis.";
RL   Plant Physiol. 139:39-51(2005).
RN   [4]
RP   SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=19725876; DOI=10.1111/j.1742-4658.2009.07258.x;
RA   Gerrard Wheeler M.C., Arias C.L., Maurino V.G., Andreo C.S.,
RA   Drincovich M.F.;
RT   "Identification of domains involved in the allosteric regulation of
RT   cytosolic Arabidopsis thaliana NADP-malic enzymes.";
RL   FEBS J. 276:5665-5677(2009).
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         Evidence={ECO:0000269|PubMed:16113210};
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         Evidence={ECO:0000269|PubMed:16113210};
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   -!- ACTIVITY REGULATION: Slightly activated by succinate and aspartate.
CC       Repressed by fumarate, malate, oxaloacetate and glucose.
CC       {ECO:0000269|PubMed:19725876}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.5 uM for NADP (at pH 7.5) {ECO:0000269|PubMed:16113210,
CC         ECO:0000269|PubMed:19725876};
CC         KM=0.83 mM for malate (at pH 7.5) {ECO:0000269|PubMed:16113210,
CC         ECO:0000269|PubMed:19725876};
CC         KM=5 mM for pyruvate (at pH 7) {ECO:0000269|PubMed:16113210,
CC         ECO:0000269|PubMed:19725876};
CC         Note=kcat is 268.1 sec(-1) with NADP and malate as substrates (at pH
CC         7.5). kcat is 237 sec(-1) with pyruvate as substrate (at pH 7).;
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:16113210,
CC         ECO:0000269|PubMed:19725876};
CC   -!- SUBUNIT: Homohexamers and homooctamers. {ECO:0000269|PubMed:16113210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19725876}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in flowers, and, to a lower
CC       extent, in stems. In leaves and stems, restricted to the trichomes and
CC       trichome basal cells. Also present in the stipules flanking the base of
CC       the inflorescence bract leaves and in the meristematic zone of
CC       developing lateral roots. In flowers, present in pollen and the
CC       abscission zone of developing siliques. {ECO:0000269|PubMed:16113210}.
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis, present in the embryo at the
CC       globular and heart stages. Detected in the central vasculature of the
CC       siliques. During germination, only observed in stipules at the shoot
CC       apex and restricted to trichomes of the primary leaves.
CC       {ECO:0000269|PubMed:16113210}.
CC   -!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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DR   EMBL; AF149413; AAD40139.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93497.1; -; Genomic_DNA.
DR   RefSeq; NP_197960.1; NM_122489.3.
DR   AlphaFoldDB; Q9XGZ0; -.
DR   SMR; Q9XGZ0; -.
DR   BioGRID; 17932; 1.
DR   STRING; 3702.AT5G25880.1; -.
DR   PaxDb; Q9XGZ0; -.
DR   PRIDE; Q9XGZ0; -.
DR   ProteomicsDB; 232209; -.
DR   EnsemblPlants; AT5G25880.1; AT5G25880.1; AT5G25880.
DR   GeneID; 832657; -.
DR   Gramene; AT5G25880.1; AT5G25880.1; AT5G25880.
DR   KEGG; ath:AT5G25880; -.
DR   Araport; AT5G25880; -.
DR   TAIR; locus:2180547; AT5G25880.
DR   eggNOG; KOG1257; Eukaryota.
DR   HOGENOM; CLU_011405_5_1_1; -.
DR   InParanoid; Q9XGZ0; -.
DR   OrthoDB; 435571at2759; -.
DR   PhylomeDB; Q9XGZ0; -.
DR   BioCyc; ARA:AT5G25880-MON; -.
DR   BRENDA; 1.1.1.40; 399.
DR   SABIO-RK; Q9XGZ0; -.
DR   PRO; PR:Q9XGZ0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9XGZ0; baseline and differential.
DR   Genevisible; Q9XGZ0; AT.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IDA:TAIR.
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; IDA:TAIR.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LYG3"
FT   CHAIN           2..588
FT                   /note="NADP-dependent malic enzyme 3"
FT                   /id="PRO_0000420151"
FT   ACT_SITE        136
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        207
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
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         303
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         332..348
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            303
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LYG3"
SQ   SEQUENCE   588 AA;  64610 MW;  C27EE353F29417A5 CRC64;
     MGTNQTQISD EYVTGNSSGV GGGISDVYGE DSATLDQLVT PWVTSVASGY TLMRDPRYNK
     GLAFTDKERD AHYITGLLPP VVLSQDVQER KVMHNLRQYT VPLQRYMALM DLQERNERLF
     YKLLIDNVEE LLPVVYTPTV GEACQKYGSI YRRPQGLYIS LKEKGKILEV LKNWPQRGIQ
     VIVVTDGERI LGLGDLGCQG MGIPVGKLSL YTALGGIRPS ACLPITIDVG TNNEKLLNNE
     FYIGLKQKRA NGEEYAEFLQ EFMCAVKQNY GEKVLVQFED FANHHAFELL SKYCSSHLVF
     NDDIQGTASV VLAGLIAAQK VLGKSLADHT FLFLGAGEAG TGIAELIALK ISKETGKPID
     ETRKKIWLVD SKGLIVSERK ESLQHFKQPW AHDHKPVKEL LAAVNAIKPT VLIGTSGVGK
     TFTKEVVEAM ATLNEKPLIL ALSNPTSQAE CTAEEAYTWT KGRAIFASGS PFDPVQYDGK
     KFTPGQANNC YIFPGLGLGL IMSGAIRVRD DMLLAASEAL ASQVTEENFA NGLIYPPFAN
     IRKISANIAA SVGAKTYELG LASNLPRPKD LVKMAESCMY SPVYRNFR
 
 
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