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Protein

Magnesium protoporphyrin IX methyltransferase, chloroplastic

Gene

CHLM

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Regulated by the folate status via an increased concentration of S-adenosyl-homocysteine (AdoHcy), a potent inhibitor of most AdoMet-dependent methyltransferases.1 Publication

Pathwayi

GO - Molecular functioni

  1. magnesium protoporphyrin IX methyltransferase activity Source: TAIR

GO - Biological processi

  1. chlorophyll biosynthetic process Source: TAIR
  2. methylation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Chlorophyll biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciARA:AT4G25080-MONOMER.
ARA:GQT-425-MONOMER.
ARA:GQT-426-MONOMER.
ARA:GQT-427-MONOMER.
ARA:GQT-428-MONOMER.
MetaCyc:AT4G25080-MONOMER.
UniPathwayiUPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Magnesium protoporphyrin IX methyltransferase, chloroplastic (EC:2.1.1.11)
Gene namesi
Name:CHLM
Ordered Locus Names:At4g25080
ORF Names:F13M23.220
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G25080.

Subcellular locationi

Plastidchloroplast membrane 1 Publication; Peripheral membrane protein 1 Publication. Plastidchloroplast thylakoid membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast envelope Source: TAIR
  3. chloroplast membrane Source: UniProtKB-SubCell
  4. chloroplast thylakoid Source: TAIR
  5. chloroplast thylakoid membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

Pathology & Biotechi

Disruption phenotypei

Lethal under normal growth conditions and stunted albino plants unable to produce seeds when grown in presence of sucrose.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939ChloroplastSequence AnalysisAdd
BLAST
Chaini40 – 312273Magnesium protoporphyrin IX methyltransferase, chloroplasticPRO_0000422668Add
BLAST

Proteomic databases

PRIDEiQ9SW18.

Expressioni

Inductioni

Up-regulated by light. Down-regulated by the herbicide R-imazethapyr.2 Publications

Gene expression databases

GenevestigatoriQ9SW18.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G25080.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9SW18.
SMRiQ9SW18. Positions 89-310.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Magnesium protoporphyrin O-methyltransferase family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG2227.
HOGENOMiHOG000154343.
InParanoidiQ9SW18.
KOiK03428.
OMAiLDVFIHY.
PhylomeDBiQ9SW18.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR010251. Mg_prot_MeTrfase.
IPR010940. Mg_prot_MeTrfase_C.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF07109. Mg-por_mtran_C. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR02021. BchM-ChlM. 1 hit.
PROSITEiPS51556. SAM_MT_MG_PIX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9SW18-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPFAPSLLSS SSSVSQFLPR FPNATRFNVT PRSRAATVVA ASVTDLAGVD
60 70 80 90 100
STTIAVLGGG SVAALAAMVS LTDPERRRKL QAEEVGGGDK EVVREYFNST
110 120 130 140 150
GFERWRKIYG ETDEVNRVQK DIRLGHAKTV ENTMLMLTED RSLAGVTVCD
160 170 180 190 200
AGCGTGLLSI PLAKEGAIVS ASDISAAMVA EAEMKAKAQL PSENLPKFEV
210 220 230 240 250
NDLESLTGKY DTVVCLDVLI HYPQNKADGM IAHLASLAEK RVILSFAPKT
260 270 280 290 300
FYYDILKRIG ELFPGPSKAT RAYLHSEADV ERALGKVGWK ISKRGLTTTQ
310
FYFSRLIEAV PM
Length:312
Mass (Da):33,796
Last modified:May 1, 2000 - v1
Checksum:i81A9C8611F2683A6
GO
Isoform 2 (identifier: Q9SW18-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.

Show »
Length:245
Mass (Da):27,148
Checksum:i255E601AB620DD8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061R → G in BAH19415 (PubMed:19423640).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6767Missing in isoform 2. 1 PublicationVSP_046549Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035523 Genomic DNA. Translation: CAB36750.1.
AL161562 Genomic DNA. Translation: CAB79417.1.
CP002687 Genomic DNA. Translation: AEE85000.1.
CP002687 Genomic DNA. Translation: AEE85001.1.
CP002687 Genomic DNA. Translation: AEE85002.1.
CP002687 Genomic DNA. Translation: AEE85003.1.
CP002687 Genomic DNA. Translation: AEE85004.1.
AY034948 mRNA. Translation: AAK59454.1.
AY062991 mRNA. Translation: AAL34165.1.
AK316688 mRNA. Translation: BAH19415.1.
AK316669 mRNA. Translation: BAH19398.1.
AK319071 mRNA. Translation: BAH57186.1.
PIRiT05529.
RefSeqiNP_001119052.1. NM_001125580.1. [Q9SW18-2]
NP_001190832.1. NM_001203903.1. [Q9SW18-1]
NP_194238.1. NM_118640.2. [Q9SW18-1]
NP_849438.1. NM_179107.1. [Q9SW18-1]
NP_849439.1. NM_179108.2. [Q9SW18-1]
UniGeneiAt.22023.

Genome annotation databases

EnsemblPlantsiAT4G25080.1; AT4G25080.1; AT4G25080. [Q9SW18-1]
AT4G25080.2; AT4G25080.2; AT4G25080. [Q9SW18-1]
AT4G25080.3; AT4G25080.3; AT4G25080. [Q9SW18-1]
AT4G25080.5; AT4G25080.5; AT4G25080. [Q9SW18-1]
GeneIDi828611.
KEGGiath:AT4G25080.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL035523 Genomic DNA. Translation: CAB36750.1.
AL161562 Genomic DNA. Translation: CAB79417.1.
CP002687 Genomic DNA. Translation: AEE85000.1.
CP002687 Genomic DNA. Translation: AEE85001.1.
CP002687 Genomic DNA. Translation: AEE85002.1.
CP002687 Genomic DNA. Translation: AEE85003.1.
CP002687 Genomic DNA. Translation: AEE85004.1.
AY034948 mRNA. Translation: AAK59454.1.
AY062991 mRNA. Translation: AAL34165.1.
AK316688 mRNA. Translation: BAH19415.1.
AK316669 mRNA. Translation: BAH19398.1.
AK319071 mRNA. Translation: BAH57186.1.
PIRiT05529.
RefSeqiNP_001119052.1. NM_001125580.1. [Q9SW18-2]
NP_001190832.1. NM_001203903.1. [Q9SW18-1]
NP_194238.1. NM_118640.2. [Q9SW18-1]
NP_849438.1. NM_179107.1. [Q9SW18-1]
NP_849439.1. NM_179108.2. [Q9SW18-1]
UniGeneiAt.22023.

3D structure databases

ProteinModelPortaliQ9SW18.
SMRiQ9SW18. Positions 89-310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G25080.1-P.

Proteomic databases

PRIDEiQ9SW18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G25080.1; AT4G25080.1; AT4G25080. [Q9SW18-1]
AT4G25080.2; AT4G25080.2; AT4G25080. [Q9SW18-1]
AT4G25080.3; AT4G25080.3; AT4G25080. [Q9SW18-1]
AT4G25080.5; AT4G25080.5; AT4G25080. [Q9SW18-1]
GeneIDi828611.
KEGGiath:AT4G25080.

Organism-specific databases

TAIRiAT4G25080.

Phylogenomic databases

eggNOGiCOG2227.
HOGENOMiHOG000154343.
InParanoidiQ9SW18.
KOiK03428.
OMAiLDVFIHY.
PhylomeDBiQ9SW18.

Enzyme and pathway databases

UniPathwayiUPA00668.
BioCyciARA:AT4G25080-MONOMER.
ARA:GQT-425-MONOMER.
ARA:GQT-426-MONOMER.
ARA:GQT-427-MONOMER.
ARA:GQT-428-MONOMER.
MetaCyc:AT4G25080-MONOMER.

Gene expression databases

GenevestigatoriQ9SW18.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR010251. Mg_prot_MeTrfase.
IPR010940. Mg_prot_MeTrfase_C.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF07109. Mg-por_mtran_C. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR02021. BchM-ChlM. 1 hit.
PROSITEiPS51556. SAM_MT_MG_PIX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    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.
    Nature 402:769-777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: cv. Columbia.
  5. "The plant S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase is located in both envelope and thylakoid chloroplast membranes."
    Block M.A., Tewari A.K., Albrieux C., Marechal E., Joyard J.
    Eur. J. Biochem. 269:240-248(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY.
  6. "Knock-out of the magnesium protoporphyrin IX methyltransferase gene in Arabidopsis. Effects on chloroplast development and on chloroplast-to-nucleus signaling."
    Pontier D., Albrieux C., Joyard J., Lagrange T., Block M.A.
    J. Biol. Chem. 282:2297-2304(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Wassilewskija.
  7. "Light signalling pathways regulating the Mg-chelatase branchpoint of chlorophyll synthesis during de-etiolation in Arabidopsis thaliana."
    Stephenson P.G., Terry M.J.
    Photochem. Photobiol. Sci. 7:1243-1252(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY LIGHT.
  8. "C1 metabolism and chlorophyll synthesis: the Mg-protoporphyrin IX methyltransferase activity is dependent on the folate status."
    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.
    New Phytol. 182:137-145(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Imazethapyr enantioselectively affects chlorophyll synthesis and photosynthesis in Arabidopsis thaliana."
    Qian H., Han X., Zhang Q., Sun Z., Sun L., Fu Z.
    J. Agric. Food Chem. 61:1172-1178(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY IMAZETHAPYR.

Entry informationi

Entry nameiCHLM_ARATH
AccessioniPrimary (citable) accession number: Q9SW18
Secondary accession number(s): B3H4K6, B9DF98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.