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Protein

5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic

Gene

MS3

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

Functioni

Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.1 Publication

Catalytic activityi

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Kineticsi

  1. KM=17 µM for 5-methyltetrahydrofolate1 Publication
  1. Vmax=0.6 nmol/min/mg enzyme toward 5-methyltetrahydrofolate1 Publication

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetE route).
Proteins known to be involved in this subpathway in this organism are:
  1. 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2 (MS2), 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic (MS3), 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1 (MS1)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetE route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei538 – 5381L-homocysteineBy similarity
Binding sitei615 – 61515-methyltetrahydrofolateBy similarity
Binding sitei653 – 6531L-homocysteineBy similarity
Metal bindingi695 – 6951Zinc 1By similarity
Metal bindingi697 – 6971Zinc 1By similarity
Metal bindingi706 – 7061Zinc 2By similarity
Metal bindingi710 – 7101Zinc 2By similarity
Metal bindingi781 – 7811Zinc 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G20980-MONOMER.
ARA:GQT-661-MONOMER.
SABIO-RKQ0WNZ5.
UniPathwayiUPA00051; UER00082.

Names & Taxonomyi

Protein namesi
Recommended name:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic (EC:2.1.1.14)
Alternative name(s):
Cobalamin-independent methionine synthase 3
Short name:
AtMS3
Gene namesi
Name:MS3
Ordered Locus Names:At5g20980
ORF Names:F22D1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G20980.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • extracellular region Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333ChloroplastSequence analysisAdd
BLAST
Chaini34 – 8127795-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplasticPRO_0000424357Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki454 – 454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ0WNZ5.
PRIDEiQ0WNZ5.

PTM databases

iPTMnetiQ0WNZ5.

Expressioni

Tissue specificityi

Expressed in seeds.1 Publication

Gene expression databases

GenevisibleiQ0WNZ5. AT.

Interactioni

Protein-protein interaction databases

IntActiQ0WNZ5. 1 interaction.
STRINGi3702.AT5G20980.1.

Structurei

3D structure databases

ProteinModelPortaliQ0WNZ5.
SMRiQ0WNZ5. Positions 50-808.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni485 – 4873L-homocysteine bindingBy similarity
Regioni569 – 57025-methyltetrahydrofolate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2263. Eukaryota.
COG0620. LUCA.
HOGENOMiHOG000246221.
InParanoidiQ0WNZ5.
KOiK00549.
OMAiAHAMEMT.
PhylomeDBiQ0WNZ5.

Family and domain databases

HAMAPiMF_00172. Meth_synth.
InterProiIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Met_Synth_C/arc.
[Graphical view]
PfamiPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsiTIGR01371. met_syn_B12ind. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q0WNZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQLALQRLQ PLASLPRRPP SLPPPSSATP SLPCATASRR PRFYVARAMS
60 70 80 90 100
SHIVGYPRIG PKRELKFALE SFWDGKTNVD DLQNVAANLR KSIWKHMAHA
110 120 130 140 150
GIKYIPSNTF SYYDQMLDTT AMLGAVPSRY GWESGEIGFD VYFSMARGNA
160 170 180 190 200
SAHAMEMTKW FDTNYHYIVP ELGPDVNFSY ASHKAVVEFK EAKALGIDTV
210 220 230 240 250
PVLIGPMTYL LLSKPAKGVE KSFCLLSLID KILPVYKEVL ADLKSAGARW
260 270 280 290 300
IQFDEPILVM DLDTSQLQAF SDAYSHMESS LAGLNVLIAT YFADVPAEAY
310 320 330 340 350
KTLMSLKCVT GFGFDLVRGL ETLDLIKMNF PRGKLLFAGV VDGRNIWAND
360 370 380 390 400
LSASLKTLQT LEDIVGKEKV VVSTSCSLLH TAVDLVNEMK LDKELKSWLA
410 420 430 440 450
FAAQKVVEVN ALAKSFSGAK DEALFSSNSM RQASRRSSPR VTNAAVQQDV
460 470 480 490 500
DAVKKSDHHR STEVSVRLQA QQKKLNLPAL PTTTIGSFPQ TTDLRRIRRE
510 520 530 540 550
FKAKKISEVD YVQTIKEEYE KVIKLQEELG IDVLVHGEAE RNDMVEFFGE
560 570 580 590 600
QLSGFAFTSN GWVQSYGSRC VKPPIIYGDI TRPKAMTVFW SSMAQKMTQR
610 620 630 640 650
PMKGMLTGPV TILNWSFVRN DQPRHETCFQ IALAIKDEVE DLEKAGVTVI
660 670 680 690 700
QIDEAALREG LPLRKSEQKF YLDWAVHAFR ITNSGVQDST QIHTHMCYSN
710 720 730 740 750
FNDIIHSIID MDADVITIEN SRSDEKLLSV FHEGVKYGAG IGPGVYDIHS
760 770 780 790 800
PRIPSTEEIA ERINKMLAVL DSKVLWVNPD CGLKTRNYSE VKSALSNMVA
810
AAKLIRSQLN KS
Length:812
Mass (Da):90,594
Last modified:September 5, 2006 - v1
Checksum:i976DC8AC06A1DF27
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111P → L in CAE55865 (PubMed:15024005).Curated
Sequence conflicti77 – 771T → S in CAE55865 (PubMed:15024005).Curated
Sequence conflicti634 – 6341A → G in CAE55865 (PubMed:15024005).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ608675 mRNA. Translation: CAE55865.1.
AF296834 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92915.1.
CP002688 Genomic DNA. Translation: AED92916.1.
AK229291 mRNA. Translation: BAF01154.1.
RefSeqiNP_001078611.1. NM_001085142.1.
NP_197598.2. NM_122107.3.
UniGeneiAt.31122.

Genome annotation databases

EnsemblPlantsiAT5G20980.1; AT5G20980.1; AT5G20980.
AT5G20980.2; AT5G20980.2; AT5G20980.
GeneIDi832223.
GrameneiAT5G20980.1; AT5G20980.1; AT5G20980.
AT5G20980.2; AT5G20980.2; AT5G20980.
KEGGiath:AT5G20980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ608675 mRNA. Translation: CAE55865.1.
AF296834 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92915.1.
CP002688 Genomic DNA. Translation: AED92916.1.
AK229291 mRNA. Translation: BAF01154.1.
RefSeqiNP_001078611.1. NM_001085142.1.
NP_197598.2. NM_122107.3.
UniGeneiAt.31122.

3D structure databases

ProteinModelPortaliQ0WNZ5.
SMRiQ0WNZ5. Positions 50-808.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ0WNZ5. 1 interaction.
STRINGi3702.AT5G20980.1.

PTM databases

iPTMnetiQ0WNZ5.

Proteomic databases

PaxDbiQ0WNZ5.
PRIDEiQ0WNZ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G20980.1; AT5G20980.1; AT5G20980.
AT5G20980.2; AT5G20980.2; AT5G20980.
GeneIDi832223.
GrameneiAT5G20980.1; AT5G20980.1; AT5G20980.
AT5G20980.2; AT5G20980.2; AT5G20980.
KEGGiath:AT5G20980.

Organism-specific databases

TAIRiAT5G20980.

Phylogenomic databases

eggNOGiKOG2263. Eukaryota.
COG0620. LUCA.
HOGENOMiHOG000246221.
InParanoidiQ0WNZ5.
KOiK00549.
OMAiAHAMEMT.
PhylomeDBiQ0WNZ5.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00082.
BioCyciARA:AT5G20980-MONOMER.
ARA:GQT-661-MONOMER.
SABIO-RKQ0WNZ5.

Miscellaneous databases

PROiQ0WNZ5.

Gene expression databases

GenevisibleiQ0WNZ5. AT.

Family and domain databases

HAMAPiMF_00172. Meth_synth.
InterProiIPR013215. Cbl-indep_Met_Synth_N.
IPR006276. Cobalamin-indep_Met_synthase.
IPR002629. Met_Synth_C/arc.
[Graphical view]
PfamiPF08267. Meth_synt_1. 1 hit.
PF01717. Meth_synt_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000382. MeTrfase_B12_ind. 1 hit.
TIGRFAMsiTIGR01371. met_syn_B12ind. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Methionine metabolism in plants: chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosol."
    Ravanel S., Block M.A., Rippert P., Jabrin S., Curien G., Rebeille F., Douce R.
    J. Biol. Chem. 279:22548-22557(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: cv. Wassilewskija.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiMETE3_ARATH
AccessioniPrimary (citable) accession number: Q0WNZ5
Secondary accession number(s): Q6KCR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2013
Last sequence update: September 5, 2006
Last modified: July 6, 2016
This is version 85 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

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 one 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.