ID   CHLM_ARATH              Reviewed;         312 AA.
AC   Q9SW18; B3H4K6; B9DF98;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Magnesium protoporphyrin IX methyltransferase, chloroplastic;
DE            EC=2.1.1.11;
DE   Flags: Precursor;
GN   Name=CHLM; OrderedLocusNames=At4g25080; ORFNames=F13M23.220;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=11784318; DOI=10.1046/j.0014-2956.2001.02643.x;
RA   Block M.A., Tewari A.K., Albrieux C., Marechal E., Joyard J.;
RT   "The plant S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase
RT   is located in both envelope and thylakoid chloroplast membranes.";
RL   Eur. J. Biochem. 269:240-248(2002).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=17135235; DOI=10.1074/jbc.m610286200;
RA   Pontier D., Albrieux C., Joyard J., Lagrange T., Block M.A.;
RT   "Knock-out of the magnesium protoporphyrin IX methyltransferase gene in
RT   Arabidopsis. Effects on chloroplast development and on chloroplast-to-
RT   nucleus signaling.";
RL   J. Biol. Chem. 282:2297-2304(2007).
RN   [7]
RP   INDUCTION BY LIGHT.
RX   PubMed=18846290; DOI=10.1039/b802596g;
RA   Stephenson P.G., Terry M.J.;
RT   "Light signalling pathways regulating the Mg-chelatase branchpoint of
RT   chlorophyll synthesis during de-etiolation in Arabidopsis thaliana.";
RL   Photochem. Photobiol. Sci. 7:1243-1252(2008).
RN   [8]
RP   ACTIVITY REGULATION.
RX   PubMed=19076298; DOI=10.1111/j.1469-8137.2008.02707.x;
RA   Van Wilder V., De Brouwer V., Loizeau K., Gambonnet B., Albrieux C.,
RA   Van Der Straeten D., Lambert W.E., Douce R., Block M.A., Rebeille F.,
RA   Ravanel S.;
RT   "C1 metabolism and chlorophyll synthesis: the Mg-protoporphyrin IX
RT   methyltransferase activity is dependent on the folate status.";
RL   New Phytol. 182:137-145(2009).
RN   [9]
RP   INDUCTION BY IMAZETHAPYR.
RX   PubMed=23343119; DOI=10.1021/jf305198g;
RA   Qian H., Han X., Zhang Q., Sun Z., Sun L., Fu Z.;
RT   "Imazethapyr enantioselectively affects chlorophyll synthesis and
RT   photosynthesis in Arabidopsis thaliana.";
RL   J. Agric. Food Chem. 61:1172-1178(2013).
CC   -!- FUNCTION: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX
CC       methylester using S-adenosyl-L-methionine as a cofactor. Involved in
CC       chloroplast-to-nucleus signaling by acting as a negative effector of
CC       nuclear photosynthetic gene expression. {ECO:0000269|PubMed:11784318,
CC       ECO:0000269|PubMed:17135235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mg-protoporphyrin IX + S-adenosyl-L-methionine = Mg-
CC         protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:17809, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:60491, ChEBI:CHEBI:60492; EC=2.1.1.11;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00889,
CC         ECO:0000269|PubMed:11784318};
CC   -!- ACTIVITY REGULATION: Regulated by the folate status via an increased
CC       concentration of S-adenosyl-homocysteine (AdoHcy), a potent inhibitor
CC       of most AdoMet-dependent methyltransferases.
CC       {ECO:0000269|PubMed:19076298}.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000269|PubMed:11784318}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11784318}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:11784318}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:11784318}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SW18-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SW18-2; Sequence=VSP_046549;
CC   -!- INDUCTION: Up-regulated by light. Down-regulated by the herbicide R-
CC       imazethapyr. {ECO:0000269|PubMed:18846290,
CC       ECO:0000269|PubMed:23343119}.
CC   -!- DISRUPTION PHENOTYPE: Lethal under normal growth conditions and stunted
CC       albino plants unable to produce seeds when grown in presence of
CC       sucrose. {ECO:0000269|PubMed:17135235}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Magnesium protoporphyrin O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00889}.
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DR   EMBL; AL035523; CAB36750.1; -; Genomic_DNA.
DR   EMBL; AL161562; CAB79417.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85000.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85001.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85002.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85003.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85004.1; -; Genomic_DNA.
DR   EMBL; AY034948; AAK59454.1; -; mRNA.
DR   EMBL; AY062991; AAL34165.1; -; mRNA.
DR   EMBL; AK316688; BAH19415.1; -; mRNA.
DR   EMBL; AK316669; BAH19398.1; -; mRNA.
DR   EMBL; AK319071; BAH57186.1; -; mRNA.
DR   PIR; T05529; T05529.
DR   RefSeq; NP_001119052.1; NM_001125580.1. [Q9SW18-2]
DR   RefSeq; NP_001190832.1; NM_001203903.1. [Q9SW18-1]
DR   RefSeq; NP_194238.1; NM_118640.3. [Q9SW18-1]
DR   RefSeq; NP_849438.1; NM_179107.2. [Q9SW18-1]
DR   RefSeq; NP_849439.1; NM_179108.3. [Q9SW18-1]
DR   AlphaFoldDB; Q9SW18; -.
DR   SMR; Q9SW18; -.
DR   BioGRID; 13898; 2.
DR   STRING; 3702.Q9SW18; -.
DR   iPTMnet; Q9SW18; -.
DR   PaxDb; 3702-AT4G25080-5; -.
DR   ProteomicsDB; 245178; -. [Q9SW18-1]
DR   EnsemblPlants; AT4G25080.1; AT4G25080.1; AT4G25080. [Q9SW18-1]
DR   EnsemblPlants; AT4G25080.2; AT4G25080.2; AT4G25080. [Q9SW18-1]
DR   EnsemblPlants; AT4G25080.3; AT4G25080.3; AT4G25080. [Q9SW18-1]
DR   EnsemblPlants; AT4G25080.4; AT4G25080.4; AT4G25080. [Q9SW18-2]
DR   EnsemblPlants; AT4G25080.5; AT4G25080.5; AT4G25080. [Q9SW18-1]
DR   GeneID; 828611; -.
DR   Gramene; AT4G25080.1; AT4G25080.1; AT4G25080. [Q9SW18-1]
DR   Gramene; AT4G25080.2; AT4G25080.2; AT4G25080. [Q9SW18-1]
DR   Gramene; AT4G25080.3; AT4G25080.3; AT4G25080. [Q9SW18-1]
DR   Gramene; AT4G25080.4; AT4G25080.4; AT4G25080. [Q9SW18-2]
DR   Gramene; AT4G25080.5; AT4G25080.5; AT4G25080. [Q9SW18-1]
DR   KEGG; ath:AT4G25080; -.
DR   Araport; AT4G25080; -.
DR   TAIR; AT4G25080; CHLM.
DR   eggNOG; KOG1270; Eukaryota.
DR   HOGENOM; CLU_066342_0_0_1; -.
DR   InParanoid; Q9SW18; -.
DR   OMA; LDVFIHY; -.
DR   PhylomeDB; Q9SW18; -.
DR   BioCyc; ARA:AT4G25080-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G25080-MONOMER; -.
DR   BRENDA; 2.1.1.11; 399.
DR   UniPathway; UPA00668; -.
DR   PRO; PR:Q9SW18; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SW18; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0046406; F:magnesium protoporphyrin IX methyltransferase activity; IDA:TAIR.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:CACAO.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR010251; Mg_prot_MeTrfase.
DR   InterPro; IPR010940; Mg_prot_MeTrfase_C.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR02021; BchM-ChlM; 1.
DR   PANTHER; PTHR43591:SF81; MAGNESIUM PROTOPORPHYRIN IX METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43591; METHYLTRANSFERASE; 1.
DR   Pfam; PF07109; Mg-por_mtran_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51556; SAM_MT_MG_PIX; 1.
DR   Genevisible; Q9SW18; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chlorophyll biosynthesis; Chloroplast; Membrane;
KW   Methyltransferase; Plastid; Reference proteome; S-adenosyl-L-methionine;
KW   Thylakoid; Transferase; Transit peptide.
FT   TRANSIT         1..39
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..312
FT                   /note="Magnesium protoporphyrin IX methyltransferase,
FT                   chloroplastic"
FT                   /id="PRO_0000422668"
FT   VAR_SEQ         1..67
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19423640"
FT                   /id="VSP_046549"
FT   CONFLICT        106
FT                   /note="R -> G (in Ref. 4; BAH19415)"
FT                   /evidence="ECO:0000305"
SQ   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
//