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P13009

- METH_ECOLI

UniProt

P13009 - METH_ECOLI

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Protein

Methionine synthase

Gene

metH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.

Catalytic activityi

5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

Cofactori

Protein has several cofactor binding sites:

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi247 – 2471Zinc
Metal bindingi310 – 3101Zinc
Metal bindingi311 – 3111Zinc
Metal bindingi759 – 7591Cobalt (cobalamin axial ligand)1 Publication
Binding sitei804 – 8041Cobalamin2 Publications
Binding sitei946 – 9461S-adenosyl-L-methionine1 Publication
Binding sitei1134 – 11341S-adenosyl-L-methionine; via carbonyl oxygen1 Publication
Binding sitei1138 – 11381Cobalamin; via carbonyl oxygen2 Publications

GO - Molecular functioni

  1. cobalamin binding Source: EcoCyc
  2. methionine synthase activity Source: EcoCyc
  3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: EcoCyc
  4. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. pteridine-containing compound metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

Cobalamin, Cobalt, Metal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:HOMOCYSMETB12-MONOMER.
ECOL316407:JW3979-MONOMER.
MetaCyc:HOMOCYSMETB12-MONOMER.
RETL1328306-WGS:GSTH-2949-MONOMER.
UniPathwayiUPA00051; UER00081.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine synthase (EC:2.1.1.13)
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Methionine synthase, vitamin-B12-dependent
Short name:
MS
Gene namesi
Name:metH
Ordered Locus Names:b4019, JW3979
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10587. metH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi310 – 3101C → A or S: Loss of zinc binding. Loss of catalytic activity. 1 Publication
Mutagenesisi311 – 3111C → A or S: Loss of zinc binding. Loss of catalytic activity. 1 Publication
Mutagenesisi757 – 7571D → E: Decreases activity by about 70%. 1 Publication
Mutagenesisi757 – 7571D → N: Decreases activity by about 45%. 1 Publication
Mutagenesisi759 – 7591H → G: Loss of catalytic activity. 1 Publication
Mutagenesisi810 – 8101S → A: Decreases activity by about 40%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12271226Methionine synthasePRO_0000204532Add
BLAST

Proteomic databases

PaxDbiP13009.
PRIDEiP13009.

2D gel databases

SWISS-2DPAGEP13009.

Expressioni

Gene expression databases

GenevestigatoriP13009.

Interactioni

Protein-protein interaction databases

IntActiP13009. 13 interactions.
STRINGi511145.b4019.

Structurei

Secondary structure

1
1227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi653 – 6564Combined sources
Helixi659 – 66911Combined sources
Helixi675 – 68511Combined sources
Beta strandi686 – 6883Combined sources
Helixi691 – 6944Combined sources
Helixi696 – 71015Combined sources
Helixi715 – 73723Combined sources
Beta strandi738 – 7414Combined sources
Beta strandi748 – 7547Combined sources
Helixi761 – 77111Combined sources
Turni772 – 7743Combined sources
Beta strandi776 – 7794Combined sources
Beta strandi782 – 7843Combined sources
Helixi786 – 79611Combined sources
Beta strandi799 – 8046Combined sources
Helixi809 – 82315Combined sources
Beta strandi830 – 8345Combined sources
Beta strandi835 – 8373Combined sources
Helixi839 – 8457Combined sources
Helixi847 – 8493Combined sources
Beta strandi854 – 8563Combined sources
Helixi860 – 87011Combined sources
Turni873 – 8753Combined sources
Helixi876 – 89318Combined sources
Helixi906 – 9116Combined sources
Helixi918 – 9203Combined sources
Beta strandi930 – 9356Combined sources
Helixi938 – 9414Combined sources
Helixi942 – 9443Combined sources
Helixi948 – 9536Combined sources
Helixi962 – 9654Combined sources
Turni967 – 9693Combined sources
Helixi970 – 99021Combined sources
Beta strandi996 – 100712Combined sources
Beta strandi1010 – 10167Combined sources
Beta strandi1022 – 10276Combined sources
Beta strandi1036 – 10383Combined sources
Helixi1043 – 10464Combined sources
Helixi1050 – 10523Combined sources
Beta strandi1057 – 10659Combined sources
Helixi1069 – 107810Combined sources
Helixi1082 – 110928Combined sources
Helixi1122 – 11265Combined sources
Beta strandi1130 – 11334Combined sources
Helixi1145 – 11473Combined sources
Helixi1148 – 11547Combined sources
Helixi1157 – 11615Combined sources
Beta strandi1167 – 11693Combined sources
Beta strandi1171 – 118212Combined sources
Helixi1197 – 120711Combined sources
Helixi1211 – 12188Combined sources
Helixi1219 – 12213Combined sources
Beta strandi1222 – 12243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMTX-ray3.00A/B651-896[»]
1K7YX-ray3.00A651-1227[»]
1K98X-ray3.75A651-1227[»]
1MSKX-ray1.80A897-1227[»]
3BULX-ray2.30A649-1227[»]
3IV9X-ray3.25A649-1227[»]
3IVAX-ray2.70A649-1227[»]
ProteinModelPortaliP13009.
SMRiP13009. Positions 6-639, 651-1227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 325324Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini356 – 617262Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini650 – 74495B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini746 – 881136B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini897 – 1227331AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni834 – 8352Cobalamin-binding
Regioni1189 – 11902S-adenosyl-L-methionine binding

Domaini

Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.1 Publication

Sequence similaritiesi

Contains 1 AdoMet activation domain.PROSITE-ProRule annotation
Contains 1 B12-binding domain.PROSITE-ProRule annotation
Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1410.
HOGENOMiHOG000251409.
InParanoidiP13009.
KOiK00548.
OMAiLTEHYAM.
OrthoDBiEOG6091CH.
PhylomeDBiP13009.

Family and domain databases

Gene3Di1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
3.40.50.280. 1 hit.
InterProiIPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
IPR004223. VitB12-dep_Met_synth_activ_dom.
[Graphical view]
PfamiPF02310. B12-binding. 1 hit.
PF02607. B12-binding_2. 1 hit.
PF02965. Met_synt_B12. 1 hit.
PF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF000381. MetH. 1 hit.
SMARTiSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsiTIGR02082. metH. 1 hit.
PROSITEiPS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
PS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13009-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSKVEQLRA QLNERILVLD GGMGTMIQSY RLNEADFRGE RFADWPCDLK
60 70 80 90 100
GNNDLLVLSK PEVIAAIHNA YFEAGADIIE TNTFNSTTIA MADYQMESLS
110 120 130 140 150
AEINFAAAKL ARACADEWTA RTPEKPRYVA GVLGPTNRTA SISPDVNDPA
160 170 180 190 200
FRNITFDGLV AAYRESTKAL VEGGADLILI ETVFDTLNAK AAVFAVKTEF
210 220 230 240 250
EALGVELPIM ISGTITDASG RTLSGQTTEA FYNSLRHAEA LTFGLNCALG
260 270 280 290 300
PDELRQYVQE LSRIAECYVT AHPNAGLPNA FGEYDLDADT MAKQIREWAQ
310 320 330 340 350
AGFLNIVGGC CGTTPQHIAA MSRAVEGLAP RKLPEIPVAC RLSGLEPLNI
360 370 380 390 400
GEDSLFVNVG ERTNVTGSAK FKRLIKEEKY SEALDVARQQ VENGAQIIDI
410 420 430 440 450
NMDEGMLDAE AAMVRFLNLI AGEPDIARVP IMIDSSKWDV IEKGLKCIQG
460 470 480 490 500
KGIVNSISMK EGVDAFIHHA KLLRRYGAAV VVMAFDEQGQ ADTRARKIEI
510 520 530 540 550
CRRAYKILTE EVGFPPEDII FDPNIFAVAT GIEEHNNYAQ DFIGACEDIK
560 570 580 590 600
RELPHALISG GVSNVSFSFR GNDPVREAIH AVFLYYAIRN GMDMGIVNAG
610 620 630 640 650
QLAIYDDLPA ELRDAVEDVI LNRRDDGTER LLELAEKYRG SKTDDTANAQ
660 670 680 690 700
QAEWRSWEVN KRLEYSLVKG ITEFIEQDTE EARQQATRPI EVIEGPLMDG
710 720 730 740 750
MNVVGDLFGE GKMFLPQVVK SARVMKQAVA YLEPFIEASK EQGKTNGKMV
760 770 780 790 800
IATVKGDVHD IGKNIVGVVL QCNNYEIVDL GVMVPAEKIL RTAKEVNADL
810 820 830 840 850
IGLSGLITPS LDEMVNVAKE MERQGFTIPL LIGGATTSKA HTAVKIEQNY
860 870 880 890 900
SGPTVYVQNA SRTVGVVAAL LSDTQRDDFV ARTRKEYETV RIQHGRKKPR
910 920 930 940 950
TPPVTLEAAR DNDFAFDWQA YTPPVAHRLG VQEVEASIET LRNYIDWTPF
960 970 980 990 1000
FMTWSLAGKY PRILEDEVVG VEAQRLFKDA NDMLDKLSAE KTLNPRGVVG
1010 1020 1030 1040 1050
LFPANRVGDD IEIYRDETRT HVINVSHHLR QQTEKTGFAN YCLADFVAPK
1060 1070 1080 1090 1100
LSGKADYIGA FAVTGGLEED ALADAFEAQH DDYNKIMVKA LADRLAEAFA
1110 1120 1130 1140 1150
EYLHERVRKV YWGYAPNENL SNEELIRENY QGIRPAPGYP ACPEHTEKAT
1160 1170 1180 1190 1200
IWELLEVEKH TGMKLTESFA MWPGASVSGW YFSHPDSKYY AVAQIQRDQV
1210 1220
EDYARRKGMS VTEVERWLAP NLGYDAD
Length:1,227
Mass (Da):135,997
Last modified:January 23, 2007 - v5
Checksum:i91F0CAA1E9127D9A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131A → R(PubMed:2185137)Curated
Sequence conflicti113 – 1131A → R(PubMed:2668277)Curated
Sequence conflicti641 – 6411S → T(PubMed:2185137)Curated
Sequence conflicti641 – 6411S → T(PubMed:2668277)Curated
Sequence conflicti1079 – 10802QH → HD in CAA34601. (PubMed:2185137)Curated
Sequence conflicti1195 – 122733IQRDQ…GYDAD → TSARSG in CAA34601. (PubMed:2185137)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16584 Genomic DNA. Translation: CAA34601.1.
J04975 Unassigned DNA. Translation: AAA02995.1.
U00006 Genomic DNA. Translation: AAC43113.1.
U00096 Genomic DNA. Translation: AAC76989.1.
AP009048 Genomic DNA. Translation: BAE78021.1.
PIRiB65209. XYECMH.
RefSeqiNP_418443.1. NC_000913.3.
YP_492162.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76989; AAC76989; b4019.
BAE78021; BAE78021; BAE78021.
GeneIDi12934458.
948522.
KEGGiecj:Y75_p3906.
eco:b4019.
PATRICi32123567. VBIEscCol129921_4132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16584 Genomic DNA. Translation: CAA34601.1 .
J04975 Unassigned DNA. Translation: AAA02995.1 .
U00006 Genomic DNA. Translation: AAC43113.1 .
U00096 Genomic DNA. Translation: AAC76989.1 .
AP009048 Genomic DNA. Translation: BAE78021.1 .
PIRi B65209. XYECMH.
RefSeqi NP_418443.1. NC_000913.3.
YP_492162.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BMT X-ray 3.00 A/B 651-896 [» ]
1K7Y X-ray 3.00 A 651-1227 [» ]
1K98 X-ray 3.75 A 651-1227 [» ]
1MSK X-ray 1.80 A 897-1227 [» ]
3BUL X-ray 2.30 A 649-1227 [» ]
3IV9 X-ray 3.25 A 649-1227 [» ]
3IVA X-ray 2.70 A 649-1227 [» ]
ProteinModelPortali P13009.
SMRi P13009. Positions 6-639, 651-1227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P13009. 13 interactions.
STRINGi 511145.b4019.

2D gel databases

SWISS-2DPAGE P13009.

Proteomic databases

PaxDbi P13009.
PRIDEi P13009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76989 ; AAC76989 ; b4019 .
BAE78021 ; BAE78021 ; BAE78021 .
GeneIDi 12934458.
948522.
KEGGi ecj:Y75_p3906.
eco:b4019.
PATRICi 32123567. VBIEscCol129921_4132.

Organism-specific databases

EchoBASEi EB0582.
EcoGenei EG10587. metH.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
InParanoidi P13009.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG6091CH.
PhylomeDBi P13009.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .
BioCyci EcoCyc:HOMOCYSMETB12-MONOMER.
ECOL316407:JW3979-MONOMER.
MetaCyc:HOMOCYSMETB12-MONOMER.
RETL1328306-WGS:GSTH-2949-MONOMER.

Miscellaneous databases

EvolutionaryTracei P13009.
PROi P13009.

Gene expression databases

Genevestigatori P13009.

Family and domain databases

Gene3Di 1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
3.40.50.280. 1 hit.
InterProi IPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
IPR004223. VitB12-dep_Met_synth_activ_dom.
[Graphical view ]
Pfami PF02310. B12-binding. 1 hit.
PF02607. B12-binding_2. 1 hit.
PF02965. Met_synt_B12. 1 hit.
PF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view ]
PIRSFi PIRSF000381. MetH. 1 hit.
SMARTi SM01018. B12-binding_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsi TIGR02082. metH. 1 hit.
PROSITEi PS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
PS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the metH gene of Escherichia coli K-12 and comparison with that of Salmonella typhimurium LT2."
    Old I.G., Margarita D., Glass R.E., Saint-Girons I.
    Gene 87:15-21(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain."
    Banerjee R.V., Johnston N.L., Sobeski J.K., Datta P., Matthews R.G.
    J. Biol. Chem. 264:13888-13895(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: K12.
  3. "Electrospray mass spectrometric analysis of the domains of a large enzyme: observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase."
    Drummond J.T., Loo R.R., Matthews R.G.
    Biochemistry 32:9282-9289(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine."
    Goulding C.W., Postigo D., Matthews R.G.
    Biochemistry 36:8082-8091(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION, DOMAIN, MUTAGENESIS OF CYS-310 AND CYS-311.
    Strain: K12.
  8. "Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli."
    Luschinsky C.L., Drummond J.T., Matthews R.G., Ludwig M.L.
    J. Mol. Biol. 225:557-560(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  9. "Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity."
    Jarrett J.T., Amaratunga M., Drennan C.L., Scholten J.D., Sands R.H., Ludwig M.L., Matthews R.G.
    Biochemistry 35:2464-2475(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-757; HIS-759 AND SER-810.
    Strain: K12.
  10. "Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation."
    Goulding C.W., Matthews R.G.
    Biochemistry 36:15749-15757(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZINC BINDING SITES.
    Strain: K12.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy."
    Peariso K., Zhou Z.S., Smith A.E., Matthews R.G., Penner-Hahn J.E.
    Biochemistry 40:987-993(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZINC BINDING SITES, ROLE OF ZINC IN SUBSTRATE BINDING.
    Strain: K12.
  13. "Cobalamin-dependent methyltransferases."
    Matthews R.G.
    Acc. Chem. Res. 34:681-689(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. "How a protein binds B12: a 3.0 A X-ray structure of B12-binding domains of methionine synthase."
    Drennan C.L., Huang S., Drummond J.T., Matthews R.G., Ludwig M.L.
    Science 266:1669-1674(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 651-896 IN COMPLEX WITH COBALAMIN.
  15. "The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12."
    Dixon M.M., Huang S., Matthews R.G., Ludwig M.L.
    Structure 4:1263-1275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 897-1227 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.
    Strain: K12.
  16. "Domain alternation switches B(12)-dependent methionine synthase to the activation conformation."
    Bandarian V., Pattridge K.A., Lennon B.W., Huddler D.P., Matthews R.G., Ludwig M.L.
    Nat. Struct. Biol. 9:53-56(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 651-1227 OF WILD-TYPE AND MUTANT GLY-759 IN COMPLEX WITH COBALAMIN.
    Strain: K12.

Entry informationi

Entry nameiMETH_ECOLI
AccessioniPrimary (citable) accession number: P13009
Secondary accession number(s): Q2M6T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 156 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

L-homocysteine is bound via the zinc atom.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3