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A8XY95

- METH_CAEBR

UniProt

A8XY95 - METH_CAEBR

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Protein

Probable methionine synthase

Gene

metr-1

Organism
Caenorhabditis briggsae
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.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi249 – 2491ZincPROSITE-ProRule annotation
Metal bindingi312 – 3121ZincPROSITE-ProRule annotation
Metal bindingi313 – 3131ZincPROSITE-ProRule annotation
Metal bindingi775 – 7751Cobalt (cobalamin axial ligand)By similarity
Binding sitei820 – 8201CobalaminBy similarity
Binding sitei977 – 9771S-adenosyl-L-methionineBy similarity
Binding sitei1171 – 11711S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei1175 – 11751Cobalamin; via carbonyl oxygenBy similarity

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:
Probable methionine synthase (EC:2.1.1.13)
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Vitamin-B12 dependent methionine synthase
Short name:
MS
Gene namesi
Name:metr-1
ORF Names:CBG20636
OrganismiCaenorhabditis briggsae
Taxonomic identifieri6238 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000008549: Chromosome II, UP000008549: Unassembled WGS sequence

Organism-specific databases

WormBaseiCBG20636; CBP26766; WBGene00039583; Cbr-metr-1.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12731273Probable methionine synthasePRO_0000412913Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi6238.CBG20636.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 327321Hcy-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini360 – 621262Pterin-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini652 – 74998B12-binding N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini762 – 897136B12-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini927 – 1273347AdoMet activationPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni850 – 8512Cobalamin-bindingBy similarity
Regioni1225 – 12262S-adenosyl-L-methionine bindingBy similarity

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 AdoMet activation domain.PROSITE-ProRule annotation
Contains 1 B12-binding domain.PROSITE-ProRule annotation
Contains 1 Hcy-binding domain.PROSITE-ProRule annotation
Contains 1 pterin-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1410.
HOGENOMiHOG000251409.
InParanoidiA8XY95.
OrthoDBiEOG7TF786.

Family and domain databases

Gene3Di1.10.1240.10. 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.
InterProiIPR003759. 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]
PfamiPF02310. 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]
PIRSFiPIRSF000381. MetH. 1 hit.
SMARTiSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMiSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsiTIGR02082. metH. 1 hit.
PROSITEiPS50974. 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]

Sequencei

Sequence statusi: Complete.

A8XY95-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRSSLFKEL ADIAKERIMI IDGAMGTMIQ REYMEEHDFR GEILKDHDKP
60 70 80 90 100
LKGNNDLLSI TRPDIIYKIH KLYLEAGADF IETNTFSGTT IAQADYHCEH
110 120 130 140 150
LVHEINYQSA LVARRACDDV GAATGIRRYV CGAIGPTNRT LSISPSVEKP
160 170 180 190 200
DFRNVTFQEL VKAYGDQARS LIQGGVDVLL VETVFDSANA KAALFAIRTL
210 220 230 240 250
FEDEGVPEIP VFLSGTIVDM SGRTLSGQTG EAFLVSTKQG KPIAVGLNCA
260 270 280 290 300
LGAKDMRQFV QNMSLWSDTL ILCYPNAGLP NALGGYDETP EEMAEVLREF
310 320 330 340 350
AQDGLVNIIG GCCGTTPDHI NAMYKAVQGI SPRVPPADPH AGKMLLSGLE
360 370 380 390 400
PSIVGPETNF VNIGERCNVA GSRRFCNLIK NENYDTAIDV ARVQVDSGAQ
410 420 430 440 450
ILDVNMDDGL LDGPYAMSKF LRLISSEPDV AKIPVCIDSS DFDVIIAGLE
460 470 480 490 500
STQGKCVVNS ISLKEGEEKF KERARIVKRY GAAVVVMAFD EEGQAAETER
510 520 530 540 550
KFEICERSYR ILTEEVGFNP NDIIFDANIL TIATGMDEHA NYGMYFIEAT
560 570 580 590 600
RMIRENLPGA HVSGGVSNIS FSFRGMEAIR EAMHSVFLFY AIKAGMDMGI
610 620 630 640 650
VNAGALPVYE DIDKPLLQLL EDLLFNRDPE ATEKLLVAAQ EMKKDGKKAD
660 670 680 690 700
TKTDEWRNTS VEERLKFALV KGIDQFVVAD TEEARQNTEK YPRPLNVIER
710 720 730 740 750
PLMDGMAVVG ELFGAGKMFL PQVIKSARVM KKAVAHLLPF MDAERQANIE
760 770 780 790 800
KMGLDEDESP YQGTVVIATV KGDVHDIGKN IVAVVLGCNN FKVVDLGVMT
810 820 830 840 850
PCENIIKAAI EEKADFIGLS GLITPSLDEM VHVAKEMNRV GLKIPLLIGG
860 870 880 890 900
ATTSKTHTAV KIAPRYPHPV VHCLDASKSV VVCSSLSDMT VRDAFLQDLN
910 920 930 940 950
EDYEDVRTKM CLVSYLNHFF ITEHYESLKD RRFVALGKTR EKKFNIDWNK
960 970 980 990 1000
FSPVKPSFIG RREFQNFDFK ELIPYIDWKP FFDVWQLRGK YPNRSYPKIF
1010 1020 1030 1040 1050
DDADVGGEAK RVFDDAQTWL KKLIDEKVLT ANAVVSFLPA ASEGDDIHVY
1060 1070 1080 1090 1100
DPETGNKLDT FYGLRQQSGR EHDQSHFCLS DFIRPLKIGV PDDYLGLFAC
1110 1120 1130 1140 1150
TAGLGAEEYC KVLEENHDDY ASIMVKALAD RLAEAYAEYL HKEVRVNLWG
1160 1170 1180 1190 1200
YSTNEQLTET DLLSIKYEGI RPACGYPSQP DHTEKRTLWK LLEAEKNGIV
1210 1220 1230 1240 1250
LTEHLAMLPA ASVSGLYFAN PQSQYFAVGK IDEDQVAFIY VRSKNVTDYA
1260 1270
ARKNVPKEEV ERWLSPIIGY ELD
Length:1,273
Mass (Da):141,762
Last modified:December 16, 2008 - v2
Checksum:i7178233645CE06AE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
HE600991 Genomic DNA. Translation: CAP37612.2.

Genome annotation databases

EnsemblMetazoaiCBG20636; CBG20636; CBG20636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
HE600991 Genomic DNA. Translation: CAP37612.2 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6238.CBG20636.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai CBG20636 ; CBG20636 ; CBG20636 .

Organism-specific databases

WormBasei CBG20636 ; CBP26766 ; WBGene00039583 ; Cbr-metr-1.

Phylogenomic databases

eggNOGi COG1410.
HOGENOMi HOG000251409.
InParanoidi A8XY95.
OrthoDBi EOG7TF786.

Enzyme and pathway databases

UniPathwayi UPA00051 ; UER00081 .

Family and domain databases

Gene3Di 1.10.1240.10. 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.
InterProi IPR003759. 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 ]
Pfami PF02310. 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 ]
PIRSFi PIRSF000381. MetH. 1 hit.
SMARTi SM01018. B12-binding_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsi TIGR02082. metH. 1 hit.
PROSITEi PS50974. 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 ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AF16.

Entry informationi

Entry nameiMETH_CAEBR
AccessioniPrimary (citable) accession number: A8XY95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: December 16, 2008
Last modified: October 29, 2014
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3