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Magnesium protoporphyrin IX methyltransferase, chloroplastic (EC 2.1.1.11)

 CHLM_ARATH              Reviewed;         312 AA.
Q9SW18; B3H4K6; B9DF98;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-FEB-2018, entry version 117.
RecName: Full=Magnesium protoporphyrin IX methyltransferase, chloroplastic;
EC=2.1.1.11;
Flags: Precursor;
Name=CHLM; OrderedLocusNames=At4g25080; ORFNames=F13M23.220;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=cv. Columbia;
PubMed=19423640; DOI=10.1093/dnares/dsp009;
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M.,
Seki M., Shinozaki K.;
"Analysis of multiple occurrences of alternative splicing events in
Arabidopsis thaliana using novel sequenced full-length cDNAs.";
DNA Res. 16:155-164(2009).
[5]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=11784318; DOI=10.1046/j.0014-2956.2001.02643.x;
Block M.A., Tewari A.K., Albrieux C., Marechal E., Joyard J.;
"The plant S-adenosyl-L-methionine:Mg-protoporphyrin IX
methyltransferase is located in both envelope and thylakoid
chloroplast membranes.";
Eur. J. Biochem. 269:240-248(2002).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Wassilewskija;
PubMed=17135235; DOI=10.1074/jbc.M610286200;
Pontier D., Albrieux C., Joyard J., Lagrange T., Block M.A.;
"Knock-out of the magnesium protoporphyrin IX methyltransferase gene
in Arabidopsis. Effects on chloroplast development and on chloroplast-
to-nucleus signaling.";
J. Biol. Chem. 282:2297-2304(2007).
[7]
INDUCTION BY LIGHT.
PubMed=18846290; DOI=10.1039/b802596g;
Stephenson P.G., Terry M.J.;
"Light signalling pathways regulating the Mg-chelatase branchpoint of
chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
Photochem. Photobiol. Sci. 7:1243-1252(2008).
[8]
ENZYME REGULATION.
PubMed=19076298; DOI=10.1111/j.1469-8137.2008.02707.x;
Van Wilder V., De Brouwer V., Loizeau K., Gambonnet B., Albrieux C.,
Van Der Straeten D., Lambert W.E., Douce R., Block M.A., Rebeille F.,
Ravanel S.;
"C1 metabolism and chlorophyll synthesis: the Mg-protoporphyrin IX
methyltransferase activity is dependent on the folate status.";
New Phytol. 182:137-145(2009).
[9]
INDUCTION BY IMAZETHAPYR.
PubMed=23343119; DOI=10.1021/jf305198g;
Qian H., Han X., Zhang Q., Sun Z., Sun L., Fu Z.;
"Imazethapyr enantioselectively affects chlorophyll synthesis and
photosynthesis in Arabidopsis thaliana.";
J. Agric. Food Chem. 61:1172-1178(2013).
-!- FUNCTION: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX
methylester using S-adenosyl-L-methionine as a cofactor. Involved
in chloroplast-to-nucleus signaling by acting as a negative
effector of nuclear photosynthetic gene expression.
{ECO:0000269|PubMed:11784318, ECO:0000269|PubMed:17135235}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + magnesium
protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium
protoporphyrin IX 13-methyl ester. {ECO:0000255|PROSITE-
ProRule:PRU00889, ECO:0000269|PubMed:11784318}.
-!- ENZYME REGULATION: Regulated by the folate status via an increased
concentration of S-adenosyl-homocysteine (AdoHcy), a potent
inhibitor of most AdoMet-dependent methyltransferases.
{ECO:0000269|PubMed:19076298}.
-!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
biosynthesis.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
{ECO:0000269|PubMed:11784318}; Peripheral membrane protein
{ECO:0000269|PubMed:11784318}. Plastid, chloroplast thylakoid
membrane {ECO:0000269|PubMed:11784318}; Peripheral membrane
protein {ECO:0000269|PubMed:11784318}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9SW18-1; Sequence=Displayed;
Name=2;
IsoId=Q9SW18-2; Sequence=VSP_046549;
-!- INDUCTION: Up-regulated by light. Down-regulated by the herbicide
R-imazethapyr. {ECO:0000269|PubMed:18846290,
ECO:0000269|PubMed:23343119}.
-!- DISRUPTION PHENOTYPE: Lethal under normal growth conditions and
stunted albino plants unable to produce seeds when grown in
presence of sucrose. {ECO:0000269|PubMed:17135235}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Magnesium protoporphyrin O-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU00889}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL035523; CAB36750.1; -; Genomic_DNA.
EMBL; AL161562; CAB79417.1; -; Genomic_DNA.
EMBL; CP002687; AEE85000.1; -; Genomic_DNA.
EMBL; CP002687; AEE85001.1; -; Genomic_DNA.
EMBL; CP002687; AEE85002.1; -; Genomic_DNA.
EMBL; CP002687; AEE85003.1; -; Genomic_DNA.
EMBL; CP002687; AEE85004.1; -; Genomic_DNA.
EMBL; AY034948; AAK59454.1; -; mRNA.
EMBL; AY062991; AAL34165.1; -; mRNA.
EMBL; AK316688; BAH19415.1; -; mRNA.
EMBL; AK316669; BAH19398.1; -; mRNA.
EMBL; AK319071; BAH57186.1; -; mRNA.
PIR; T05529; T05529.
RefSeq; NP_001119052.1; NM_001125580.1. [Q9SW18-2]
RefSeq; NP_001190832.1; NM_001203903.1. [Q9SW18-1]
RefSeq; NP_194238.1; NM_118640.3. [Q9SW18-1]
RefSeq; NP_849438.1; NM_179107.2. [Q9SW18-1]
RefSeq; NP_849439.1; NM_179108.3. [Q9SW18-1]
UniGene; At.22023; -.
ProteinModelPortal; Q9SW18; -.
SMR; Q9SW18; -.
BioGrid; 13898; 2.
STRING; 3702.AT4G25080.1; -.
PaxDb; Q9SW18; -.
PRIDE; Q9SW18; -.
EnsemblPlants; AT4G25080.1; AT4G25080.1; AT4G25080. [Q9SW18-1]
EnsemblPlants; AT4G25080.2; AT4G25080.2; AT4G25080. [Q9SW18-1]
EnsemblPlants; AT4G25080.3; AT4G25080.3; AT4G25080. [Q9SW18-1]
EnsemblPlants; AT4G25080.4; AT4G25080.4; AT4G25080. [Q9SW18-2]
EnsemblPlants; AT4G25080.5; AT4G25080.5; AT4G25080. [Q9SW18-1]
GeneID; 828611; -.
Gramene; AT4G25080.1; AT4G25080.1; AT4G25080. [Q9SW18-1]
Gramene; AT4G25080.2; AT4G25080.2; AT4G25080. [Q9SW18-1]
Gramene; AT4G25080.3; AT4G25080.3; AT4G25080. [Q9SW18-1]
Gramene; AT4G25080.4; AT4G25080.4; AT4G25080. [Q9SW18-2]
Gramene; AT4G25080.5; AT4G25080.5; AT4G25080. [Q9SW18-1]
KEGG; ath:AT4G25080; -.
Araport; AT4G25080; -.
TAIR; locus:2117388; AT4G25080.
eggNOG; KOG1270; Eukaryota.
eggNOG; COG2227; LUCA.
HOGENOM; HOG000154343; -.
InParanoid; Q9SW18; -.
KO; K03428; -.
OMA; LDVFIHY; -.
OrthoDB; EOG09360INC; -.
PhylomeDB; Q9SW18; -.
BioCyc; ARA:AT4G25080-MONOMER; -.
BioCyc; MetaCyc:AT4G25080-MONOMER; -.
UniPathway; UPA00668; -.
PRO; PR:Q9SW18; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9SW18; baseline and differential.
Genevisible; Q9SW18; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0046406; F:magnesium protoporphyrin IX methyltransferase activity; IDA:TAIR.
GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:CACAO.
InterPro; IPR010251; Mg_prot_MeTrfase.
InterPro; IPR010940; Mg_prot_MeTrfase_C.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR43591:SF9; PTHR43591:SF9; 1.
Pfam; PF07109; Mg-por_mtran_C; 1.
SUPFAM; SSF53335; SSF53335; 1.
TIGRFAMs; TIGR02021; BchM-ChlM; 1.
PROSITE; PS51556; SAM_MT_MG_PIX; 1.
1: Evidence at protein level;
Alternative splicing; Chlorophyll biosynthesis; Chloroplast;
Complete proteome; Membrane; Methyltransferase; Plastid;
Reference proteome; S-adenosyl-L-methionine; Thylakoid; Transferase;
Transit peptide.
TRANSIT 1 39 Chloroplast. {ECO:0000255}.
CHAIN 40 312 Magnesium protoporphyrin IX
methyltransferase, chloroplastic.
/FTId=PRO_0000422668.
VAR_SEQ 1 67 Missing (in isoform 2).
{ECO:0000303|PubMed:19423640}.
/FTId=VSP_046549.
CONFLICT 106 106 R -> G (in Ref. 4; BAH19415).
{ECO:0000305}.
SEQUENCE 312 AA; 33796 MW; 81A9C8611F2683A6 CRC64;
MPFAPSLLSS SSSVSQFLPR FPNATRFNVT PRSRAATVVA ASVTDLAGVD STTIAVLGGG
SVAALAAMVS LTDPERRRKL QAEEVGGGDK EVVREYFNST GFERWRKIYG ETDEVNRVQK
DIRLGHAKTV ENTMLMLTED RSLAGVTVCD AGCGTGLLSI PLAKEGAIVS ASDISAAMVA
EAEMKAKAQL PSENLPKFEV NDLESLTGKY DTVVCLDVLI HYPQNKADGM IAHLASLAEK
RVILSFAPKT FYYDILKRIG ELFPGPSKAT RAYLHSEADV ERALGKVGWK ISKRGLTTTQ
FYFSRLIEAV PM


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