Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9SW18

- CHLM_ARATH

UniProt

Q9SW18 - CHLM_ARATH

Protein

Magnesium protoporphyrin IX methyltransferase, chloroplastic

Gene

CHLM

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 PublicationPROSITE-ProRule annotation

    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

    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: 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

    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

    ArrayExpressiQ9SW18.
    GenevestigatoriQ9SW18.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G25080.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SW18.
    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.
    OMAiKFEVNDL.
    PhylomeDBiQ9SW18.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR010251. Mg_prot_MeTrfase.
    IPR010940. Mg_prot_MeTrfase_C.
    IPR029063. SAM-dependent_MTases-like.
    [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. Align

    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

    MPFAPSLLSS SSSVSQFLPR FPNATRFNVT PRSRAATVVA ASVTDLAGVD    50
    STTIAVLGGG SVAALAAMVS LTDPERRRKL QAEEVGGGDK EVVREYFNST 100
    GFERWRKIYG ETDEVNRVQK DIRLGHAKTV ENTMLMLTED RSLAGVTVCD 150
    AGCGTGLLSI PLAKEGAIVS ASDISAAMVA EAEMKAKAQL PSENLPKFEV 200
    NDLESLTGKY DTVVCLDVLI HYPQNKADGM IAHLASLAEK RVILSFAPKT 250
    FYYDILKRIG ELFPGPSKAT RAYLHSEADV ERALGKVGWK ISKRGLTTTQ 300
    FYFSRLIEAV PM 312
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T05529.
    RefSeqi NP_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 ]
    UniGenei At.22023.

    3D structure databases

    ProteinModelPortali Q9SW18.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G25080.1-P.

    Proteomic databases

    PRIDEi Q9SW18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G25080.1 ; 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 ]
    GeneIDi 828611.
    KEGGi ath:AT4G25080.

    Organism-specific databases

    TAIRi AT4G25080.

    Phylogenomic databases

    eggNOGi COG2227.
    HOGENOMi HOG000154343.
    InParanoidi Q9SW18.
    KOi K03428.
    OMAi KFEVNDL.
    PhylomeDBi Q9SW18.

    Enzyme and pathway databases

    UniPathwayi UPA00668 .
    BioCyci ARA:AT4G25080-MONOMER.
    ARA:GQT-425-MONOMER.
    ARA:GQT-426-MONOMER.
    ARA:GQT-427-MONOMER.
    ARA:GQT-428-MONOMER.
    MetaCyc:AT4G25080-MONOMER.

    Gene expression databases

    ArrayExpressi Q9SW18.
    Genevestigatori Q9SW18.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR010251. Mg_prot_MeTrfase.
    IPR010940. Mg_prot_MeTrfase_C.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF07109. Mg-por_mtran_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    TIGRFAMsi TIGR02021. BchM-ChlM. 1 hit.
    PROSITEi PS51556. SAM_MT_MG_PIX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-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(2003) [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(2009) [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(2002) [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(2007) [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(2008) [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(2009) [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(2013) [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: October 1, 2014
    This is version 97 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