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O33465 (METH_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 61. 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
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length607 AA.
Sequence statusFragment.
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 Potential.

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 Hcy-binding domain.

Contains 1 pterin-binding domain.

Caution

Ser-314 is present instead of the conserved Cys which is expected to be a zinc-binding residue.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›607›607Methionine synthase
PRO_0000204535

Regions

Domain8 – 328321Hcy-binding
Domain359 – ›607›249Pterin-binding

Sites

Metal binding2501Zinc Potential
Metal binding3131Zinc Potential

Experimental info

Non-terminal residue6071

Sequences

Sequence LengthMass (Da)Tools
O33465 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: BB7743CC28A922B3

FASTA60765,840
        10         20         30         40         50         60 
MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS DVKGNNDLLL 

        70         80         90        100        110        120 
LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME SLVYELNVEG ARIARQVADA 

       130        140        150        160        170        180 
KTLETPDKPR FVAGVLGPTS RTCSISPDVN DPGYRNVTFD ELVENYIEAT RGLIEGGADL 

       190        200        210        220        230        240 
ILIETIFDTL NAKAAIFAVQ QVFEEDAVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH 

       250        260        270        280        290        300 
AKPISVGLNC ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE 

       310        320        330        340        350        360 
FAASGFLNII GGCSGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP FTIDGQSLFV 

       370        380        390        400        410        420 
NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV IDINMDEGML DSQAAMVRFL 

       430        440        450        460        470        480 
NMIAGEPDIS RVPIMIDSSK GEVIEAGLKC IQGKGIVNSI SMKEGVEQFK HHARLCKRYG 

       490        500        510        520        530        540 
AAVVVMAFDE VGQADTAARK KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN 

       550        560        570        580        590        600 
YAVDFIEACA YIRDHLPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA ISNGLTMGIV 


NAGLLEI 

« Hide

References

[1]"Cis-trans isomerization of unsaturated fatty acids: cloning and sequencing of the cti gene from Pseudomonas putida P8."
Holtwick R., Meinhardt F., Keweloh H.
Appl. Environ. Microbiol. 63:4292-4297(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: P8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000978 Genomic DNA. Translation: CAA04437.1.

3D structure databases

ProteinModelPortalO33465.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00051; UER00081.

Family and domain databases

Gene3D3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
InterProIPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
[Graphical view]
PfamPF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFPIRSF000381. MetH. 1 hit.
SUPFAMSSF51717. SSF51717. 1 hit.
SSF82282. SSF82282. 1 hit.
PROSITEPS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETH_PSEPU
AccessionPrimary (citable) accession number: O33465
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: October 16, 2013
This is version 61 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