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Q9Z2Q4 (METH_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Vitamin-B12 dependent methionine synthase
Short name=MS
Gene names
Name:Mtr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1253 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Subcellular location

Cytoplasm By similarity.

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 – 12531253Methionine synthase
PRO_0000312902

Regions

Domain6 – 326321Hcy-binding
Domain359 – 620262Pterin-binding
Domain650 – 74798B12-binding N-terminal
Domain760 – 895136B12-binding
Domain911 – 1253343AdoMet activation
Region848 – 8492Cobalamin-binding By similarity
Region1215 – 12162S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2481Zinc By similarity
Metal binding3111Zinc By similarity
Metal binding3121Zinc By similarity
Metal binding7731Cobalt (cobalamin axial ligand) By similarity
Binding site8181Cobalamin By similarity
Binding site9621S-adenosyl-L-methionine By similarity
Binding site11601S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11641Cobalamin; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z2Q4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 96BD40B796EBD75B

FASTA1,253139,164
        10         20         30         40         50         60 
MKKTLQDEIE AILRKRIMVL DGGMGTMIQR YKLSEENFQG QEFKDHSRPL KGNNDILSIT 

        70         80         90        100        110        120 
QPDVIYQIHK EYLLAGADII ETNTFSSTSI AQADYGLEHL AYRMNKCSAD VARKAAEEIT 

       130        140        150        160        170        180 
LQTGVKRFVA GSLGPTNKTL SVSPSVERPD YRNITFDELV EAYQEQAKGL LDGGVDILLI 

       190        200        210        220        230        240 
ETIFDTANAK AALFALQKLF EENYASPRPI FISGTIVDKS GRTLSGQTGE AFVTSVSHSD 

       250        260        270        280        290        300 
PLCIGLNCAL GAAEMRPFIE TIGKCTTAYV LCYPNAGLPN TFGDYDETPA MMAMHLKDFA 

       310        320        330        340        350        360 
VDGLVNVVGG CCGSTPDHIR EIAEAVKNCK PRVPPDSVFE GHMLLSGLEP FRIGPYTNFV 

       370        380        390        400        410        420 
NIGERCNVAG SKKFAKLIMA GNYEEALSVA KVQVEMGAQV LDINMDDGML DGPSAMTKFC 

       430        440        450        460        470        480 
NFIASEPDIA KVPLCIDSSN FAVIEAGLKC CQGKCIVNSI SLKEGEEDFL EKARKIKKFG 

       490        500        510        520        530        540 
AAVVVMAFDE EGQATETDVK VSVCTRAYHL LVEKVGFNPN DIIFDPNILT IGTGMEEHNL 

       550        560        570        580        590        600 
YAINFIHATR VIKETLPGVR ISGGLSNLSF AFRGMDAIRE AMHGVFLYHA IKFGMDMGIV 

       610        620        630        640        650        660 
NAGSLPVYDD IHKDLLQLCE DLIWNRDAEA TEKLLRYAQT HGKGGKKVIQ TDEWRNGSIE 

       670        680        690        700        710        720 
ERLEYALVKG IEKHIVEDTE EARLNREKYP RPLNIIEGPL MNGMKVVGDL FGAGKMFLPQ 

       730        740        750        760        770        780 
VIKSARVMKK AVGHLIPFME KEREEARVLN GSVEEEDPYQ GTIVLATVKG DVHDIGKNIV 

       790        800        810        820        830        840 
GVVLGCNNFR VIDLGVMTPC DKILQAALDH KADIIGLSGL ITPSLDEMIF VAKEMERLAI 

       850        860        870        880        890        900 
KIPLLIGGAT TSRTHTAVKI APRYSAPVIH VLDASKSVVV CSQLLDENLK DDYFEEILEE 

       910        920        930        940        950        960 
YEDIRQDHYE SLKERKYLPL SQARKHSFHI DWLSEPHPVK PTFIGTQVFE DYNLQKLVDY 

       970        980        990       1000       1010       1020 
IDWKPFFDVW QLRGKYPNRG FPKIFNDKAV GEEARKVYED AQNMLSILIS RKKLRARGVV 

      1030       1040       1050       1060       1070       1080 
GFWPAQSVQD DIHLYAEGAV PQAAEPIATF YGLRQQAEKD SSSTDPYHCL SDFVAPLHSG 

      1090       1100       1110       1120       1130       1140 
VRDYLGLFAV ACFGVEELSK AYEDDGDDYS SIMVKALGDR LAEAFAEELH ERVRRELWAY 

      1150       1160       1170       1180       1190       1200 
CGSEQLGVTD LRKLRYEGIR PAPGYPSQPD HTEKLTMWRL ANIEQATGIR LTESLAMAPA 

      1210       1220       1230       1240       1250 
SAVSGLYFSN VKSKYFAVGK ISKDQIEDYA LRKNMSVAEV EKWLGPILGY DTD

« Hide

References

[1]"Cloning, sequencing, and heterologous expression of rat methionine synthase cDNA."
Yamada K., Tobimatsu T., Toraya T.
Biosci. Biotechnol. Biochem. 62:2155-2160(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF034214 mRNA. Translation: AAD05384.1.
IPIIPI00327267.
PIRT42376.
RefSeqNP_110491.1. NM_030864.1.
UniGeneRn.205061.

3D structure databases

HSSPHSSP built from PDB template 1BMT based on UniProtKB P13009.
ProteinModelPortalQ9Z2Q4.
SMRQ9Z2Q4. Positions 652-908, 914-1252.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Z2Q4. 1 interaction.
STRING10116.ENSRNOP00000023973.

PTM databases

PhosphoSiteQ9Z2Q4.

Proteomic databases

PaxDbQ9Z2Q4.
PRIDEQ9Z2Q4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81522.
KEGGrno:81522.
UCSCRGD:621283. rat.

Organism-specific databases

CTD4548.
RGD621283. Mtr.

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251409.
HOVERGENHBG006347.
InParanoidQ9Z2Q4.
KOK00548.
OrthoDBEOG41JZBC.

Enzyme and pathway databases

UniPathwayUPA00051; UER00081.

Gene expression databases

ArrayExpressQ9Z2Q4.
GenevestigatorQ9Z2Q4.

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]
PANTHERPTHR21091:SF9. PTHR21091:SF9. 1 hit.
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]
SUPFAMSSF52242. Cbl-bd. 1 hit.
SSF51717. DHP_synth_like. 1 hit.
SSF56507. Met_synth_B12. 1 hit.
SSF47644. Met_synth_Cbl-bd. 1 hit.
SSF82282. S_methyl_trans. 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...

Other

NextBio615041.

Entry information

Entry nameMETH_RAT
AccessionPrimary (citable) accession number: Q9Z2Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 1999
Last modified: April 3, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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