CHLM_ARATH
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 03-AUG-2022, entry version 135.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.AT4G25080.5; -.
DR PaxDb; Q9SW18; -.
DR PRIDE; Q9SW18; -.
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; locus:2117388; AT4G25080.
DR eggNOG; KOG1270; Eukaryota.
DR HOGENOM; CLU_066342_0_0_1; -.
DR InParanoid; Q9SW18; -.
DR OMA; LDVFIHY; -.
DR PhylomeDB; Q9SW18; -.
DR BioCyc; ARA:AT4G25080-MON; -.
DR BioCyc; MetaCyc:AT4G25080-MON; -.
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 Genevisible; Q9SW18; AT.
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:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IMP:CACAO.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR010251; Mg_prot_MeTrfase.
DR InterPro; IPR010940; Mg_prot_MeTrfase_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07109; Mg-por_mtran_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02021; BchM-ChlM; 1.
DR PROSITE; PS51556; SAM_MT_MG_PIX; 1.
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
