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Q9I2Q2

- METH_PSEAE

UniProt

Q9I2Q2 - METH_PSEAE

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Protein

Methionine synthase

Gene
metH, PA1843
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 By similarity.

Catalytic activityi

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

Cofactori

Methylcobalamin (MeCBL) By similarity.
Binds 1 zinc ion per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi254 – 2541Zinc By similarity
Metal bindingi317 – 3171Zinc By similarity
Metal bindingi318 – 3181Zinc By similarity
Metal bindingi765 – 7651Cobalt (cobalamin axial ligand) By similarity
Binding sitei810 – 8101Cobalamin By similarity
Binding sitei954 – 9541S-adenosyl-L-methionine By similarity
Binding sitei1142 – 11421S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei1146 – 11461Cobalamin; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. cobalamin binding Source: UniProtKB-KW
  2. methionine synthase activity Source: UniProtKB-EC
  3. S-adenosylmethionine-homocysteine S-methyltransferase activity Source: InterPro
  4. zinc ion binding Source: InterPro

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

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:PA1843
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA1843.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12341234Methionine synthasePRO_0000287780Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi208964.PA1843.

Structurei

3D structure databases

ProteinModelPortaliQ9I2Q2.
SMRiQ9I2Q2. Positions 19-646, 658-1233.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 332321Hcy-bindingAdd
BLAST
Domaini363 – 624262Pterin-bindingAdd
BLAST
Domaini655 – 74995B12-binding N-terminalAdd
BLAST
Domaini752 – 888137B12-bindingAdd
BLAST
Domaini904 – 1234331AdoMet activationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni840 – 8412Cobalamin-binding By similarity
Regioni1197 – 11982S-adenosyl-L-methionine binding By similarity

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 By similarity.

Sequence similaritiesi

Contains 1 B12-binding domain.
Contains 1 Hcy-binding domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1410.
HOGENOMiHOG000251409.
KOiK00548.
OMAiLTEHYAM.
OrthoDBiEOG6091CH.
PhylomeDBiQ9I2Q2.

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.

Q9I2Q2-1 [UniParc]FASTAAdd to Basket

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MSSPLTDRSA RLQALQHALR ERILILDGGM GTMIQSYKLE EADYRGERFA     50
DWPSDVKGNN DLLLLSRPDV IQAIEKAYLD AGADILETNT FNATQVSQAD 100
YGMQSLAYEL NVEGARLARQ VADAKTAETP DKPRFVAGVL GPTSRTCSIS 150
PDVNNPGYRN VTFDELVENY VEATRGLIEG GADLILIETI FDTLNAKAAI 200
FAVQGVFEEL GVELPIMISG TITDASGRTL SGQTTEAFWN SVRHARPISV 250
GLNCALGAKE LRPYIEELST KADTHVSAHP NAGLPNAFGE YDESPAEMAV 300
VVEEFAAAGF LNIVGGCCGT TPAHIEAIAK AVAKYPPRAI PEIPRACRLS 350
GLEPFTIDRS SLFVNVGERT NITGSAKFAR LIREENYAEA LEVAQQQVEA 400
GAQVIDINMD EGMLDSKAAM VTFLNLIASE PDISRVPIMI DSSKWEVIEA 450
GLKCIQGKGI VNSISMKEGV EAFKHHARLC KRYGAAVVVM AFDEDGQADT 500
QARKEEICKR SYDILVDEVG FPPEDIIFDA NIFAIATGIE EHNNYAVDFI 550
NACAYIRDNL PYALSSGGVS NVSFSFRGNN PVREAIHSVF LYYAIRNGLT 600
MGIVNAGQLE IYDEIPKALR DRVEDVVLNR TPEATEALLA IADDYKGGGA 650
VKEAEDEEWR SYSVEKRLEH ALVKGITTWI VEDTEECRQQ CARPIEVIEG 700
PLMSGMNVVG DLFGAGKMFL PQVVKSARVM KQAVAHLIPF IEAEKGDKPE 750
AKGKILMATV KGDVHDIGKN IVGVVLGCNG YDVVDLGVMV PAEKILQTAI 800
AEKCDIIGLS GLITPSLDEM VHVAKEMQRQ NFQLPLMIGG ATTSKAHTAV 850
KIDPQYSNDA VVYVTDASRA VGVATSLLSK ELKADYVART RADYAVVRER 900
TANRSARTER LSYEQAIANK PAFDWAGYQA PTPSFTGVRV LDEIDLAVLA 950
EYIDWTPFFI SWDLAGKYPR ILTDEVVGEA ATSLFNDAQA MLKKLIDEKL 1000
IKARAVFGFW PANQVEHDDL EVYGADGETL ATLHHLRQQT IKPDGKPNLS 1050
LADFVAPKES GVRDYIGGFI TTAGIGAEEV AKAYEAKGDD YNSIMVKALA 1100
DRLAEACAEW LHERVRKEYW GYARDEHLDN EALIKEQYVG IRPAPGYPAC 1150
PDHTEKGTLF ELLDPQGLSG VSLTEHYAMF PAAAVSGWYF AHPQAQYFAV 1200
GKIDKDQVER YSQRKGQEAS VSERWLAPNL GYDD 1234
Length:1,234
Mass (Da):135,063
Last modified:March 1, 2001 - v1
Checksum:i9877F8AC8BEF44ED
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG05232.1.
PIRiE83415.
RefSeqiNP_250534.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG05232; AAG05232; PA1843.
GeneIDi880631.
KEGGipae:PA1843.
PATRICi19838071. VBIPseAer58763_1916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG05232.1 .
PIRi E83415.
RefSeqi NP_250534.1. NC_002516.2.

3D structure databases

ProteinModelPortali Q9I2Q2.
SMRi Q9I2Q2. Positions 19-646, 658-1233.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA1843.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG05232 ; AAG05232 ; PA1843 .
GeneIDi 880631.
KEGGi pae:PA1843.
PATRICi 19838071. VBIPseAer58763_1916.

Organism-specific databases

PseudoCAPi PA1843.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
KOi K00548.
OMAi LTEHYAM.
OrthoDBi EOG6091CH.
PhylomeDBi Q9I2Q2.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiMETH_PSEAE
AccessioniPrimary (citable) accession number: Q9I2Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 87 of the entry and version 1 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 By similarity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi