SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O33465

- METH_PSEPU

UniProt

O33465 - METH_PSEPU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Methionine synthase

Gene
metH
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
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 Reviewed prediction.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi250 – 2501Zinc Reviewed prediction
Metal bindingi313 – 3131Zinc Reviewed prediction

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
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›607›607Methionine synthasePRO_0000204535Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO33465.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 328321Hcy-bindingAdd
BLAST
Domaini359 – ›607›249Pterin-bindingAdd
BLAST

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 Hcy-binding domain.

Family and domain databases

Gene3Di3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
InterProiIPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
[Graphical view]
PfamiPF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFiPIRSF000381. MetH. 1 hit.
SUPFAMiSSF51717. SSF51717. 1 hit.
SSF82282. SSF82282. 1 hit.
PROSITEiPS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O33465-1 [UniParc]FASTAAdd to Basket

« Hide

MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS    50
DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME 100
SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN 150
DPGYRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ 200
QVFEEDAVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC 250
ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE 300
FAASGFLNII GGCSGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP 350
FTIDGQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV 400
IDINMDEGML DSQAAMVRFL NMIAGEPDIS RVPIMIDSSK GEVIEAGLKC 450
IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK 500
KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA 550
YIRDHLPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA ISNGLTMGIV 600
NAGLLEI 607
Length:607
Mass (Da):65,840
Last modified:January 1, 1998 - v1
Checksum:iBB7743CC28A922B3
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei607 – 6071

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ000978 Genomic DNA. Translation: CAA04437.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ000978 Genomic DNA. Translation: CAA04437.1 .

3D structure databases

ProteinModelPortali O33465.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .

Family and domain databases

Gene3Di 3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
InterProi IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
[Graphical view ]
Pfami PF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view ]
PIRSFi PIRSF000381. MetH. 1 hit.
SUPFAMi SSF51717. SSF51717. 1 hit.
SSF82282. SSF82282. 1 hit.
PROSITEi PS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMETH_PSEPU
AccessioniPrimary (citable) accession number: O33465
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 62 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.

Caution

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

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