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O33465

- METH_PSEPU

UniProt

O33465 - METH_PSEPU

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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).By similarity

Catalytic activityi

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

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi250 – 2501ZincPROSITE-ProRule annotation
Metal bindingi313 – 3131ZincPROSITE-ProRule annotation

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 328321Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini359 – ›607›249Pterin-bindingPROSITE-ProRule annotationAdd
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).By similarity

Sequence similaritiesi

Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MSDRSARLQA LQNALKERIL ILDGGMGTMI QSYRLEEHDY RGTRFADWPS
60 70 80 90 100
DVKGNNDLLL LSRPDVIAAI EKAYLDAGAD ILETNTFNAT QISQADYGME
110 120 130 140 150
SLVYELNVEG ARIARQVADA KTLETPDKPR FVAGVLGPTS RTCSISPDVN
160 170 180 190 200
DPGYRNVTFD ELVENYIEAT RGLIEGGADL ILIETIFDTL NAKAAIFAVQ
210 220 230 240 250
QVFEEDAVEL PIMISGTITD ASGRTLSGQT TEAFWNSVRH AKPISVGLNC
260 270 280 290 300
ALGAKDLRPY LEELSTKADT HVSAHPNAGL PNAFGEYDET PAEMAAVVEE
310 320 330 340 350
FAASGFLNII GGCSGTTPGH IQAIAEAVAK YKPREIPEIA KACRLSGLEP
360 370 380 390 400
FTIDGQSLFV NVGERTNITG SAKFARLIRE ENYTEALEVA LQQVEAGAQV
410 420 430 440 450
IDINMDEGML DSQAAMVRFL NMIAGEPDIS RVPIMIDSSK GEVIEAGLKC
460 470 480 490 500
IQGKGIVNSI SMKEGVEQFK HHARLCKRYG AAVVVMAFDE VGQADTAARK
510 520 530 540 550
KEICKRSYDI LVNEVGFPPE DIIFDPNIFA VATGIEEHNN YAVDFIEACA
560 570 580 590 600
YIRDHLPHAL TSGGVSNVSF SFRGNNPVRE AIHSVFLFHA ISNGLTMGIV

NAGLLEI
Length:607
Mass (Da):65,840
Last modified:January 1, 1998 - v1
Checksum:iBB7743CC28A922B3
GO

Experimental Info

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: October 1, 2014
This is version 63 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.Curated

Documents

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

External Data

Dasty 3