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5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1 (EC 2.1.1.14) (Cobalamin-independent methionine synthase 1) (AtMS1) (Vitamin-B12-independent methionine synthase 1)

 METE1_ARATH             Reviewed;         765 AA.
O50008; Q6KCR2; Q8H162; Q93ZK3;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-APR-2018, entry version 151.
RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1;
EC=2.1.1.14;
AltName: Full=Cobalamin-independent methionine synthase 1;
Short=AtMS1;
AltName: Full=Vitamin-B12-independent methionine synthase 1;
Name=MS1; Synonyms=CIMS; OrderedLocusNames=At5g17920; ORFNames=MPI7.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=cv. Columbia;
PubMed=9636232; DOI=10.1073/pnas.95.13.7805;
Ravanel S., Gakiere B., Job D., Douce R.;
"The specific features of methionine biosynthesis and metabolism in
plants.";
Proc. Natl. Acad. Sci. U.S.A. 95:7805-7812(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Gakiere B., Job D., Douce R., Ravanel S.;
"Characterization of the cDNA and gene for a cytosolic cobalamin-
independent methionine synthase in Arabidopsis thaliana.";
(er) Plant Gene Register PGR99-115(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=cv. Wassilewskija;
PubMed=15024005; DOI=10.1074/jbc.M313250200;
Ravanel S., Block M.A., Rippert P., Jabrin S., Curien G., Rebeille F.,
Douce R.;
"Methionine metabolism in plants: chloroplasts are autonomous for de
novo methionine synthesis and can import S-adenosylmethionine from the
cytosol.";
J. Biol. Chem. 279:22548-22557(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH
5-METHYLTETRAHYDROFOLATE; METHIONINE AND ZINC IONS.
PubMed=15326182; DOI=10.1074/jbc.C400325200;
Ferrer J.L., Ravanel S., Robert M., Dumas R.;
"Crystal structures of cobalamin-independent methionine synthase
complexed with zinc, homocysteine, and methyltetrahydrofolate.";
J. Biol. Chem. 279:44235-44238(2004).
-!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
methyltetrahydrofolate to homocysteine resulting in methionine
formation. {ECO:0000269|PubMed:15024005}.
-!- CATALYTIC ACTIVITY: 5-methyltetrahydropteroyltri-L-glutamate + L-
homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=60 uM for 5-methyltetrahydrofolate
{ECO:0000269|PubMed:15024005};
Vmax=26.5 nmol/min/mg enzyme toward 5-methyltetrahydrofolate
{ECO:0000269|PubMed:15024005};
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-methionine from L-homocysteine (MetE route): step
1/1.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:15024005}.
-!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, siliques
and seeds. {ECO:0000269|PubMed:15024005}.
-!- SIMILARITY: Belongs to the vitamin-B12 independent methionine
synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; U97200; AAC50037.1; -; mRNA.
EMBL; AJ608673; CAE55863.1; -; mRNA.
EMBL; AB011480; BAB11226.1; -; Genomic_DNA.
EMBL; CP002688; AED92486.1; -; Genomic_DNA.
EMBL; CP002688; AED92487.1; -; Genomic_DNA.
EMBL; AF370522; AAK43899.1; -; mRNA.
EMBL; AY048201; AAK82464.1; -; mRNA.
EMBL; AY056098; AAL06986.1; -; mRNA.
EMBL; AY057478; AAL09712.1; -; mRNA.
EMBL; AY057499; AAL09740.1; -; mRNA.
EMBL; AY069876; AAL47432.1; -; mRNA.
EMBL; AY070771; AAL50108.1; -; mRNA.
EMBL; AY091692; AAM10291.1; -; mRNA.
EMBL; BT000691; AAN31836.1; -; mRNA.
RefSeq; NP_001078599.1; NM_001085130.2.
RefSeq; NP_197294.1; NM_121798.4.
UniGene; At.22340; -.
UniGene; At.24550; -.
UniGene; At.71028; -.
PDB; 1U1H; X-ray; 2.55 A; A=1-765.
PDB; 1U1J; X-ray; 2.40 A; A=1-765.
PDB; 1U1U; X-ray; 2.95 A; A=1-765.
PDB; 1U22; X-ray; 2.65 A; A=1-765.
PDBsum; 1U1H; -.
PDBsum; 1U1J; -.
PDBsum; 1U1U; -.
PDBsum; 1U22; -.
ProteinModelPortal; O50008; -.
SMR; O50008; -.
BioGrid; 16936; 8.
IntAct; O50008; 2.
MINT; O50008; -.
STRING; 3702.AT5G17920.1; -.
iPTMnet; O50008; -.
SWISS-2DPAGE; O50008; -.
PaxDb; O50008; -.
PRIDE; O50008; -.
EnsemblPlants; AT5G17920.1; AT5G17920.1; AT5G17920.
EnsemblPlants; AT5G17920.2; AT5G17920.2; AT5G17920.
GeneID; 831660; -.
Gramene; AT5G17920.1; AT5G17920.1; AT5G17920.
Gramene; AT5G17920.2; AT5G17920.2; AT5G17920.
KEGG; ath:AT5G17920; -.
Araport; AT5G17920; -.
TAIR; locus:2170318; AT5G17920.
eggNOG; KOG2263; Eukaryota.
eggNOG; COG0620; LUCA.
HOGENOM; HOG000246221; -.
InParanoid; O50008; -.
KO; K00549; -.
OMA; GRNIWKN; -.
OrthoDB; EOG093602ZG; -.
PhylomeDB; O50008; -.
BioCyc; ARA:AT5G17920-MONOMER; -.
BRENDA; 2.1.1.14; 399.
SABIO-RK; O50008; -.
UniPathway; UPA00051; UER00082.
EvolutionaryTrace; O50008; -.
PRO; PR:O50008; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; O50008; baseline and differential.
Genevisible; O50008; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IBA:GO_Central.
GO; GO:0005507; F:copper ion binding; IDA:TAIR.
GO; GO:0008705; F:methionine synthase activity; IDA:TAIR.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0050667; P:homocysteine metabolic process; IBA:GO_Central.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IEP:TAIR.
GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
Gene3D; 3.20.20.210; -; 4.
HAMAP; MF_00172; Meth_synth; 1.
InterPro; IPR013215; Cbl-indep_Met_Synth_N.
InterPro; IPR006276; Cobalamin-indep_Met_synthase.
InterPro; IPR002629; Met_Synth_C/arc.
InterPro; IPR038071; UROD/MetE-like_sf.
Pfam; PF08267; Meth_synt_1; 1.
Pfam; PF01717; Meth_synt_2; 1.
PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
SUPFAM; SSF51726; SSF51726; 2.
TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm;
Metal-binding; Methionine biosynthesis; Methyltransferase;
Reference proteome; Transferase; Zinc.
CHAIN 1 765 5-methyltetrahydropteroyltriglutamate--
homocysteine methyltransferase 1.
/FTId=PRO_0000098696.
REGION 437 439 L-homocysteine binding.
REGION 521 522 5-methyltetrahydrofolate binding.
METAL 647 647 Zinc 1.
METAL 649 649 Zinc 1.
METAL 658 658 Zinc 2.
METAL 662 662 Zinc 2.
METAL 733 733 Zinc 1.
BINDING 490 490 L-homocysteine.
BINDING 567 567 5-methyltetrahydrofolate.
{ECO:0000269|PubMed:15326182}.
BINDING 605 605 L-homocysteine.
CONFLICT 270 270 R -> L (in Ref. 6; AAL09712).
{ECO:0000305}.
CONFLICT 282 282 F -> S (in Ref. 3; CAE55863).
{ECO:0000305}.
CONFLICT 295 295 G -> R (in Ref. 6; AAN31836).
{ECO:0000305}.
CONFLICT 351 351 L -> M (in Ref. 3; CAE55863).
{ECO:0000305}.
CONFLICT 442 442 Q -> R (in Ref. 6; AAN31836).
{ECO:0000305}.
HELIX 16 26 {ECO:0000244|PDB:1U1J}.
HELIX 31 51 {ECO:0000244|PDB:1U1J}.
STRAND 58 60 {ECO:0000244|PDB:1U1J}.
HELIX 67 74 {ECO:0000244|PDB:1U1J}.
HELIX 80 82 {ECO:0000244|PDB:1U1J}.
STRAND 86 88 {ECO:0000244|PDB:1U1J}.
HELIX 91 99 {ECO:0000244|PDB:1U1J}.
STRAND 102 104 {ECO:0000244|PDB:1U1J}.
STRAND 109 111 {ECO:0000244|PDB:1U1J}.
STRAND 118 120 {ECO:0000244|PDB:1U1J}.
HELIX 136 146 {ECO:0000244|PDB:1U1J}.
STRAND 152 156 {ECO:0000244|PDB:1U1J}.
HELIX 158 163 {ECO:0000244|PDB:1U1J}.
STRAND 169 171 {ECO:0000244|PDB:1U1U}.
HELIX 177 180 {ECO:0000244|PDB:1U1J}.
HELIX 181 197 {ECO:0000244|PDB:1U1J}.
STRAND 202 206 {ECO:0000244|PDB:1U1J}.
HELIX 208 211 {ECO:0000244|PDB:1U1J}.
HELIX 216 228 {ECO:0000244|PDB:1U1J}.
TURN 230 233 {ECO:0000244|PDB:1U1J}.
STRAND 235 241 {ECO:0000244|PDB:1U1J}.
HELIX 249 255 {ECO:0000244|PDB:1U1J}.
STRAND 263 270 {ECO:0000244|PDB:1U1J}.
HELIX 274 280 {ECO:0000244|PDB:1U1J}.
STRAND 287 293 {ECO:0000244|PDB:1U1J}.
STRAND 295 297 {ECO:0000244|PDB:1U1J}.
HELIX 303 316 {ECO:0000244|PDB:1U1J}.
STRAND 322 328 {ECO:0000244|PDB:1U1J}.
HELIX 330 332 {ECO:0000244|PDB:1U1J}.
HELIX 337 339 {ECO:0000244|PDB:1U1J}.
HELIX 345 348 {ECO:0000244|PDB:1U1J}.
HELIX 354 368 {ECO:0000244|PDB:1U1J}.
HELIX 374 389 {ECO:0000244|PDB:1U1J}.
TURN 391 393 {ECO:0000244|PDB:1U1J}.
HELIX 397 400 {ECO:0000244|PDB:1U1J}.
TURN 401 405 {ECO:0000244|PDB:1U1J}.
STRAND 411 413 {ECO:0000244|PDB:1U1H}.
HELIX 416 418 {ECO:0000244|PDB:1U1J}.
HELIX 420 426 {ECO:0000244|PDB:1U1J}.
HELIX 463 479 {ECO:0000244|PDB:1U1J}.
STRAND 484 486 {ECO:0000244|PDB:1U1J}.
HELIX 498 501 {ECO:0000244|PDB:1U1J}.
STRAND 504 508 {ECO:0000244|PDB:1U22}.
STRAND 515 518 {ECO:0000244|PDB:1U1J}.
STRAND 521 523 {ECO:0000244|PDB:1U1J}.
HELIX 541 546 {ECO:0000244|PDB:1U1J}.
STRAND 554 559 {ECO:0000244|PDB:1U1J}.
HELIX 561 566 {ECO:0000244|PDB:1U1J}.
STRAND 568 570 {ECO:0000244|PDB:1U1J}.
STRAND 572 574 {ECO:0000244|PDB:1U1H}.
HELIX 576 596 {ECO:0000244|PDB:1U1J}.
STRAND 601 605 {ECO:0000244|PDB:1U1J}.
TURN 607 612 {ECO:0000244|PDB:1U1H}.
HELIX 617 619 {ECO:0000244|PDB:1U1J}.
HELIX 620 635 {ECO:0000244|PDB:1U1J}.
STRAND 640 647 {ECO:0000244|PDB:1U1J}.
TURN 654 656 {ECO:0000244|PDB:1U1J}.
HELIX 657 661 {ECO:0000244|PDB:1U1J}.
STRAND 666 669 {ECO:0000244|PDB:1U1J}.
STRAND 672 675 {ECO:0000244|PDB:1U1J}.
HELIX 679 683 {ECO:0000244|PDB:1U1J}.
TURN 684 687 {ECO:0000244|PDB:1U1J}.
STRAND 691 693 {ECO:0000244|PDB:1U1J}.
STRAND 696 698 {ECO:0000244|PDB:1U1J}.
STRAND 702 704 {ECO:0000244|PDB:1U1J}.
HELIX 708 720 {ECO:0000244|PDB:1U1J}.
STRAND 724 727 {ECO:0000244|PDB:1U22}.
STRAND 735 738 {ECO:0000244|PDB:1U1J}.
HELIX 740 759 {ECO:0000244|PDB:1U1J}.
SEQUENCE 765 AA; 84357 MW; 2EA01908B5951154 CRC64;
MASHIVGYPR MGPKRELKFA LESFWDGKST AEDLQKVSAD LRSSIWKQMS AAGTKFIPSN
TFAHYDQVLD TTAMLGAVPP RYGYTGGEIG LDVYFSMARG NASVPAMEMT KWFDTNYHYI
VPELGPEVNF SYASHKAVNE YKEAKALGVD TVPVLVGPVS YLLLSKAAKG VDKSFELLSL
LPKILPIYKE VITELKAAGA TWIQLDEPVL VMDLEGQKLQ AFTGAYAELE STLSGLNVLV
ETYFADIPAE AYKTLTSLKG VTAFGFDLVR GTKTLDLVKA GFPEGKYLFA GVVDGRNIWA
NDFAASLSTL QALEGIVGKD KLVVSTSCSL LHTAVDLINE TKLDDEIKSW LAFAAQKVVE
VNALAKALAG QKDEALFSAN AAALASRRSS PRVTNEGVQK AAAALKGSDH RRATNVSARL
DAQQKKLNLP ILPTTTIGSF PQTVELRRVR REYKAKKVSE EDYVKAIKEE IKKVVDLQEE
LDIDVLVHGE PERNDMVEYF GEQLSGFAFT ANGWVQSYGS RCVKPPVIYG DVSRPKAMTV
FWSAMAQSMT SRPMKGMLTG PVTILNWSFV RNDQPRHETC YQIALAIKDE VEDLEKGGIG
VIQIDEAALR EGLPLRKSEH AFYLDWAVHS FRITNCGVQD STQIHTHMCY SHFNDIIHSI
IDMDADVITI ENSRSDEKLL SVFREGVKYG AGIGPGVYDI HSPRIPSSEE IADRVNKMLA
VLEQNILWVN PDCGLKTRKY TEVKPALKNM VDAAKLIRSQ LASAK


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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