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Q9I2Q2 (METH_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine synthase

EC=2.1.1.13
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Methionine synthase, vitamin-B12 dependent
Short name=MS
Gene names
Name:metH
Ordered Locus Names:PA1843
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length1234 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Cofactor

Methylcobalamin (MeCBL) By similarity.

Binds 1 zinc ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Domain

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.

Miscellaneous

L-homocysteine is bound via the zinc atom By similarity.

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Contains 1 AdoMet activation domain.

Contains 1 B12-binding domain.

Contains 1 B12-binding N-terminal domain.

Contains 1 Hcy-binding domain.

Contains 1 pterin-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12341234Methionine synthase
PRO_0000287780

Regions

Domain12 – 332321Hcy-binding
Domain363 – 624262Pterin-binding
Domain655 – 74995B12-binding N-terminal
Domain752 – 888137B12-binding
Domain904 – 1234331AdoMet activation
Region840 – 8412Cobalamin-binding By similarity
Region1197 – 11982S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2541Zinc By similarity
Metal binding3171Zinc By similarity
Metal binding3181Zinc By similarity
Metal binding7651Cobalt (cobalamin axial ligand) By similarity
Binding site8101Cobalamin By similarity
Binding site9541S-adenosyl-L-methionine By similarity
Binding site11421S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11461Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I2Q2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9877F8AC8BEF44ED

FASTA1,234135,063
        10         20         30         40         50         60 
MSSPLTDRSA RLQALQHALR ERILILDGGM GTMIQSYKLE EADYRGERFA DWPSDVKGNN 

        70         80         90        100        110        120 
DLLLLSRPDV IQAIEKAYLD AGADILETNT FNATQVSQAD YGMQSLAYEL NVEGARLARQ 

       130        140        150        160        170        180 
VADAKTAETP DKPRFVAGVL GPTSRTCSIS PDVNNPGYRN VTFDELVENY VEATRGLIEG 

       190        200        210        220        230        240 
GADLILIETI FDTLNAKAAI FAVQGVFEEL GVELPIMISG TITDASGRTL SGQTTEAFWN 

       250        260        270        280        290        300 
SVRHARPISV GLNCALGAKE LRPYIEELST KADTHVSAHP NAGLPNAFGE YDESPAEMAV 

       310        320        330        340        350        360 
VVEEFAAAGF LNIVGGCCGT TPAHIEAIAK AVAKYPPRAI PEIPRACRLS GLEPFTIDRS 

       370        380        390        400        410        420 
SLFVNVGERT NITGSAKFAR LIREENYAEA LEVAQQQVEA GAQVIDINMD EGMLDSKAAM 

       430        440        450        460        470        480 
VTFLNLIASE PDISRVPIMI DSSKWEVIEA GLKCIQGKGI VNSISMKEGV EAFKHHARLC 

       490        500        510        520        530        540 
KRYGAAVVVM AFDEDGQADT QARKEEICKR SYDILVDEVG FPPEDIIFDA NIFAIATGIE 

       550        560        570        580        590        600 
EHNNYAVDFI NACAYIRDNL PYALSSGGVS NVSFSFRGNN PVREAIHSVF LYYAIRNGLT 

       610        620        630        640        650        660 
MGIVNAGQLE IYDEIPKALR DRVEDVVLNR TPEATEALLA IADDYKGGGA VKEAEDEEWR 

       670        680        690        700        710        720 
SYSVEKRLEH ALVKGITTWI VEDTEECRQQ CARPIEVIEG PLMSGMNVVG DLFGAGKMFL 

       730        740        750        760        770        780 
PQVVKSARVM KQAVAHLIPF IEAEKGDKPE AKGKILMATV KGDVHDIGKN IVGVVLGCNG 

       790        800        810        820        830        840 
YDVVDLGVMV PAEKILQTAI AEKCDIIGLS GLITPSLDEM VHVAKEMQRQ NFQLPLMIGG 

       850        860        870        880        890        900 
ATTSKAHTAV KIDPQYSNDA VVYVTDASRA VGVATSLLSK ELKADYVART RADYAVVRER 

       910        920        930        940        950        960 
TANRSARTER LSYEQAIANK PAFDWAGYQA PTPSFTGVRV LDEIDLAVLA EYIDWTPFFI 

       970        980        990       1000       1010       1020 
SWDLAGKYPR ILTDEVVGEA ATSLFNDAQA MLKKLIDEKL IKARAVFGFW PANQVEHDDL 

      1030       1040       1050       1060       1070       1080 
EVYGADGETL ATLHHLRQQT IKPDGKPNLS LADFVAPKES GVRDYIGGFI TTAGIGAEEV 

      1090       1100       1110       1120       1130       1140 
AKAYEAKGDD YNSIMVKALA DRLAEACAEW LHERVRKEYW GYARDEHLDN EALIKEQYVG 

      1150       1160       1170       1180       1190       1200 
IRPAPGYPAC PDHTEKGTLF ELLDPQGLSG VSLTEHYAMF PAAAVSGWYF AHPQAQYFAV 

      1210       1220       1230 
GKIDKDQVER YSQRKGQEAS VSERWLAPNL GYDD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG05232.1.
PIRE83415.
RefSeqNP_250534.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ9I2Q2.
SMRQ9I2Q2. Positions 19-1233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA1843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880631.
KEGGpae:PA1843.
PATRIC19838071. VBIPseAer58763_1916.

Organism-specific databases

PseudoCAPPA1843.

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251409.
KOK00548.
OMASMKEGEA.
OrthoDBEOG6091CH.
ProtClustDBPRK09490.

Enzyme and pathway databases

UniPathwayUPA00051; UER00081.

Family and domain databases

Gene3D1.10.1240.10. 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.
InterProIPR003759. 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]
PfamPF02310. 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]
PIRSFPIRSF000381. MetH. 1 hit.
SMARTSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsTIGR02082. metH. 1 hit.
PROSITEPS50974. 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]
ProtoNetSearch...

Entry information

Entry nameMETH_PSEAE
AccessionPrimary (citable) accession number: Q9I2Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways