Skip Header

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

Methionine synthase

Gene

MTR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Protein has several cofactor binding sites:

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-methionine from L-homocysteine (MetH route).
Proteins known to be involved in this subpathway in this organism are:
  1. Methionine synthase (MTR)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-methionine from L-homocysteine (MetH route), the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi260ZincPROSITE-ProRule annotation1
Metal bindingi323ZincPROSITE-ProRule annotation1
Metal bindingi324ZincPROSITE-ProRule annotation1
Metal bindingi785Cobalt (cobalamin axial ligand)By similarity1
Binding sitei830CobalaminBy similarity1
Binding sitei974S-adenosyl-L-methionineBy similarity1
Binding sitei1172S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei1176Cobalamin; via carbonyl oxygenBy similarity1

GO - Molecular functioni

GO - Biological processi

  • axon regeneration Source: BHF-UCL
  • cellular response to nitric oxide Source: BHF-UCL
  • cobalamin metabolic process Source: BHF-UCL
  • methionine biosynthetic process Source: BHF-UCL
  • methylation Source: Reactome
  • nervous system development Source: ProtInc
  • pteridine-containing compound metabolic process Source: InterPro
  • response to axon injury Source: BHF-UCL
  • sulfur amino acid metabolic process Source: Reactome
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

BioCyciMetaCyc:HS04076-MONOMER.
ZFISH:HS04076-MONOMER.
ReactomeiR-HSA-156581. Methylation.
R-HSA-1614635. Sulfur amino acid metabolism.
R-HSA-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-HSA-3359467. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
R-HSA-3359469. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.
UniPathwayiUPA00051; UER00081.

Names & Taxonomyi

Protein namesi
Recommended name:
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:MTR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7468. MTR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Homocystinuria-megaloblastic anemia, cblG complementation type (HMAG)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive inborn error of metabolism resulting from defects in the cobalamin-dependent pathway that converts homocysteine to methionine. It causes delayed psychomotor development, megaloblastic anemia, homocystinuria, and hypomethioninemia.
See also OMIM:250940
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004328881Missing in HMAG. 2 Publications1
Natural variantiVAR_004330920H → D in HMAG. 1 PublicationCorresponds to variant rs28933097dbSNPEnsembl.1
Natural variantiVAR_0043311173P → L in HMAG. 1 PublicationCorresponds to variant rs121913578dbSNPEnsembl.1
Neural tube defects, folate-sensitive (NTDFS)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionThe most common NTDs are open spina bifida (myelomeningocele) and anencephaly.
See also OMIM:601634

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4548.
MalaCardsiMTR.
MIMi250940. phenotype.
601634. phenotype.
603174. phenotype.
OpenTargetsiENSG00000116984.
Orphaneti2170. Methylcobalamin deficiency type cblG.
PharmGKBiPA31272.

Chemistry databases

ChEMBLiCHEMBL2150844.
DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.
DB00134. L-Methionine.
DB00116. Tetrahydrofolic acid.

Polymorphism and mutation databases

BioMutaiMTR.
DMDMi2842762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002045301 – 1265Methionine synthaseAdd BLAST1265

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1264PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99707.
MaxQBiQ99707.
PaxDbiQ99707.
PeptideAtlasiQ99707.
PRIDEiQ99707.

PTM databases

iPTMnetiQ99707.
PhosphoSitePlusiQ99707.

Expressioni

Tissue specificityi

Widely expressed. Expressed at the highest levels in pancreas, heart, brain, skeletal muscle and placenta. Expressed at lower levels in lung, liver and kidney.

Gene expression databases

BgeeiENSG00000116984.
CleanExiHS_MTR.
ExpressionAtlasiQ99707. baseline and differential.
GenevisibleiQ99707. HS.

Organism-specific databases

HPAiHPA044474.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MMACHCQ9Y4U13EBI-1045782,EBI-9775184

Protein-protein interaction databases

BioGridi110642. 31 interactors.
DIPiDIP-40306N.
IntActiQ99707. 8 interactors.
STRINGi9606.ENSP00000355536.

Chemistry databases

BindingDBiQ99707.

Structurei

Secondary structure

11265
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 28Combined sources11
Helixi37 – 44Combined sources8
Helixi49 – 51Combined sources3
Helixi67 – 69Combined sources3
Helixi70 – 73Combined sources4
Helixi75 – 87Combined sources13
Beta strandi92 – 94Combined sources3
Helixi102 – 105Combined sources4
Helixi106 – 108Combined sources3
Helixi111 – 113Combined sources3
Helixi114 – 136Combined sources23
Beta strandi141 – 146Combined sources6
Beta strandi153 – 155Combined sources3
Beta strandi159 – 161Combined sources3
Helixi169 – 185Combined sources17
Beta strandi189 – 198Combined sources10
Helixi199 – 213Combined sources15
Turni214 – 216Combined sources3
Beta strandi222 – 226Combined sources5
Helixi241 – 248Combined sources8
Helixi249 – 251Combined sources3
Beta strandi254 – 263Combined sources10
Turni264 – 267Combined sources4
Helixi268 – 275Combined sources8
Beta strandi279 – 287Combined sources9
Beta strandi318 – 320Combined sources3
Helixi328 – 338Combined sources11
Turni348 – 353Combined sources6
Beta strandi355 – 365Combined sources11
Beta strandi372 – 375Combined sources4
Turni380 – 382Combined sources3
Helixi384 – 391Combined sources8
Helixi395 – 407Combined sources13
Beta strandi411 – 416Combined sources6
Helixi424 – 437Combined sources14
Helixi439 – 442Combined sources4
Beta strandi446 – 449Combined sources4
Helixi453 – 462Combined sources10
Beta strandi468 – 472Combined sources5
Helixi478 – 491Combined sources14
Beta strandi494 – 501Combined sources8
Helixi509 – 527Combined sources19
Helixi531 – 533Combined sources3
Beta strandi534 – 537Combined sources4
Helixi548 – 552Combined sources5
Helixi553 – 567Combined sources15
Helixi577 – 584Combined sources8
Helixi588 – 605Combined sources18
Beta strandi609 – 612Combined sources4
Helixi620 – 622Combined sources3
Helixi625 – 635Combined sources11
Helixi642 – 648Combined sources7
Helixi932 – 937Combined sources6
Helixi944 – 946Combined sources3
Beta strandi956 – 962Combined sources7
Helixi966 – 970Combined sources5
Helixi976 – 987Combined sources12
Helixi995 – 998Combined sources4
Helixi1005 – 1022Combined sources18
Beta strandi1026 – 1040Combined sources15
Beta strandi1043 – 1046Combined sources4
Helixi1053 – 1055Combined sources3
Beta strandi1059 – 1063Combined sources5
Helixi1082 – 1085Combined sources4
Helixi1089 – 1091Combined sources3
Beta strandi1095 – 1106Combined sources12
Helixi1107 – 1116Combined sources10
Helixi1120 – 1147Combined sources28
Turni1152 – 1155Combined sources4
Helixi1160 – 1164Combined sources5
Beta strandi1168 – 1171Combined sources4
Helixi1185 – 1192Combined sources8
Helixi1195 – 1199Combined sources5
Beta strandi1209 – 1220Combined sources12
Helixi1235 – 1245Combined sources11
Helixi1249 – 1255Combined sources7
Helixi1257 – 1259Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O2KX-ray1.60A/B925-1265[»]
4CCZX-ray2.70A16-657[»]
ProteinModelPortaliQ99707.
SMRiQ99707.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99707.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 338Hcy-bindingPROSITE-ProRule annotationAdd BLAST320
Domaini371 – 632Pterin-bindingPROSITE-ProRule annotationAdd BLAST262
Domaini662 – 759B12-binding N-terminalPROSITE-ProRule annotationAdd BLAST98
Domaini772 – 907B12-bindingPROSITE-ProRule annotationAdd BLAST136
Domaini923 – 1265AdoMet activationPROSITE-ProRule annotationAdd BLAST343

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni860 – 861Cobalamin-bindingBy similarity2
Regioni1227 – 1228S-adenosyl-L-methionine bindingBy similarity2

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 B12-binding N-terminal 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

eggNOGiKOG1579. Eukaryota.
COG0646. LUCA.
COG1410. LUCA.
GeneTreeiENSGT00420000029824.
HOGENOMiHOG000251409.
HOVERGENiHBG006347.
InParanoidiQ99707.
KOiK00548.
OMAiDYNSIMV.
OrthoDBiEOG091G00WU.
PhylomeDBiQ99707.
TreeFamiTF312829.

Family and domain databases

CDDicd02069. methionine_synthase_B12_BD. 1 hit.
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.
IPR003726. HCY_dom.
IPR033706. Met_synthase_B12-bd.
IPR011822. MetH.
IPR000489. Pterin-binding_dom.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99707-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH
60 70 80 90 100
FRGQEFKDHA RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS
110 120 130 140 150
TSIAQADYGL EHLAYRMNMC SAGVARKAAE EVTLQTGIKR FVAGALGPTN
160 170 180 190 200
KTLSVSPSVE RPDYRNITFD ELVEAYQEQA KGLLDGGVDI LLIETIFDTA
210 220 230 240 250
NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT GEGFVISVSH
260 270 280 290 300
GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET
310 320 330 340 350
PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA
360 370 380 390 400
FEGHMLLSGL EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC
410 420 430 440 450
VAKVQVEMGA QVLDVNMDDG MLDGPSAMTR FCNLIASEPD IAKVPLCIDS
460 470 480 490 500
SNFAVIEAGL KCCQGKCIVN SISLKEGEDD FLEKARKIKK YGAAMVVMAF
510 520 530 540 550
DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI LTIGTGMEEH
560 570 580 590 600
NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY
610 620 630 640 650
HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA
660 670 680 690 700
QTQGTGGKKV IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK
710 720 730 740 750
YPRPLNIIEG PLMNGMKIVG DLFGAGKMFL PQVIKSARVM KKAVGHLIPF
760 770 780 790 800
MEKEREETRV LNGTVEEEDP YQGTIVLATV KGDVHDIGKN IVGVVLGCNN
810 820 830 840 850
FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM IFVAKEMERL
860 870 880 890 900
AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN
910 920 930 940 950
LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP
960 970 980 990 1000
VKPTFIGTQV FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK
1010 1020 1030 1040 1050
TVGGEARKVY DDAHNMLNTL ISQKKLRARG VVGFWPAQSI QDDIHLYAEA
1060 1070 1080 1090 1100
AVPQAAEPIA TFYGLRQQAE KDSASTEPYY CLSDFIAPLH SGIRDYLGLF
1110 1120 1130 1140 1150
AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE LHERVRRELW
1160 1170 1180 1190 1200
AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG
1210 1220 1230 1240 1250
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA
1260
EVEKWLGPIL GYDTD
Length:1,265
Mass (Da):140,527
Last modified:July 1, 1997 - v2
Checksum:iB04C26BCBE9A57C2
GO
Isoform 2 (identifier: Q99707-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     682-732: Missing.

Note: No experimental confirmation available.
Show »
Length:1,214
Mass (Da):134,793
Checksum:i2E568CD852B22E8C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05003352R → Q.Corresponds to variant rs12749581dbSNPEnsembl.1
Natural variantiVAR_00432661R → K.1 Publication1
Natural variantiVAR_004327255C → Y.1 PublicationCorresponds to variant rs1140598dbSNPEnsembl.1
Natural variantiVAR_061338314D → N.Corresponds to variant rs2229274dbSNPEnsembl.1
Natural variantiVAR_004328881Missing in HMAG. 2 Publications1
Natural variantiVAR_004329919D → G.4 PublicationsCorresponds to variant rs1805087dbSNPEnsembl.1
Natural variantiVAR_004330920H → D in HMAG. 1 PublicationCorresponds to variant rs28933097dbSNPEnsembl.1
Natural variantiVAR_0043311173P → L in HMAG. 1 PublicationCorresponds to variant rs121913578dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_057283682 – 732Missing in isoform 2. 1 PublicationAdd BLAST51

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71285 mRNA. Translation: AAC51188.1.
U75743 mRNA. Translation: AAB58906.1.
U73338 mRNA. Translation: AAB39704.1.
AL359185, AL359259 Genomic DNA. Translation: CAH73198.1.
AL359259, AL359185 Genomic DNA. Translation: CAH70983.1.
CH471098 Genomic DNA. Translation: EAW70066.1.
BC130616 mRNA. Translation: AAI30617.1.
BC136440 mRNA. Translation: AAI36441.1.
BC144095 mRNA. Translation: AAI44096.1.
CCDSiCCDS1614.1. [Q99707-1]
CCDS73054.1. [Q99707-2]
RefSeqiNP_000245.2. NM_000254.2. [Q99707-1]
NP_001278868.1. NM_001291939.1. [Q99707-2]
NP_001278869.1. NM_001291940.1.
UniGeneiHs.498187.

Genome annotation databases

EnsembliENST00000366577; ENSP00000355536; ENSG00000116984. [Q99707-1]
ENST00000535889; ENSP00000441845; ENSG00000116984. [Q99707-2]
GeneIDi4548.
KEGGihsa:4548.
UCSCiuc001hyi.5. human. [Q99707-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

5-methyltetrahydrofolate-homocysteine methyltransferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71285 mRNA. Translation: AAC51188.1.
U75743 mRNA. Translation: AAB58906.1.
U73338 mRNA. Translation: AAB39704.1.
AL359185, AL359259 Genomic DNA. Translation: CAH73198.1.
AL359259, AL359185 Genomic DNA. Translation: CAH70983.1.
CH471098 Genomic DNA. Translation: EAW70066.1.
BC130616 mRNA. Translation: AAI30617.1.
BC136440 mRNA. Translation: AAI36441.1.
BC144095 mRNA. Translation: AAI44096.1.
CCDSiCCDS1614.1. [Q99707-1]
CCDS73054.1. [Q99707-2]
RefSeqiNP_000245.2. NM_000254.2. [Q99707-1]
NP_001278868.1. NM_001291939.1. [Q99707-2]
NP_001278869.1. NM_001291940.1.
UniGeneiHs.498187.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O2KX-ray1.60A/B925-1265[»]
4CCZX-ray2.70A16-657[»]
ProteinModelPortaliQ99707.
SMRiQ99707.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110642. 31 interactors.
DIPiDIP-40306N.
IntActiQ99707. 8 interactors.
STRINGi9606.ENSP00000355536.

Chemistry databases

BindingDBiQ99707.
ChEMBLiCHEMBL2150844.
DrugBankiDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.
DB00134. L-Methionine.
DB00116. Tetrahydrofolic acid.

PTM databases

iPTMnetiQ99707.
PhosphoSitePlusiQ99707.

Polymorphism and mutation databases

BioMutaiMTR.
DMDMi2842762.

Proteomic databases

EPDiQ99707.
MaxQBiQ99707.
PaxDbiQ99707.
PeptideAtlasiQ99707.
PRIDEiQ99707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366577; ENSP00000355536; ENSG00000116984. [Q99707-1]
ENST00000535889; ENSP00000441845; ENSG00000116984. [Q99707-2]
GeneIDi4548.
KEGGihsa:4548.
UCSCiuc001hyi.5. human. [Q99707-1]

Organism-specific databases

CTDi4548.
DisGeNETi4548.
GeneCardsiMTR.
GeneReviewsiMTR.
HGNCiHGNC:7468. MTR.
HPAiHPA044474.
MalaCardsiMTR.
MIMi156570. gene.
250940. phenotype.
601634. phenotype.
603174. phenotype.
neXtProtiNX_Q99707.
OpenTargetsiENSG00000116984.
Orphaneti2170. Methylcobalamin deficiency type cblG.
PharmGKBiPA31272.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1579. Eukaryota.
COG0646. LUCA.
COG1410. LUCA.
GeneTreeiENSGT00420000029824.
HOGENOMiHOG000251409.
HOVERGENiHBG006347.
InParanoidiQ99707.
KOiK00548.
OMAiDYNSIMV.
OrthoDBiEOG091G00WU.
PhylomeDBiQ99707.
TreeFamiTF312829.

Enzyme and pathway databases

UniPathwayiUPA00051; UER00081.
BioCyciMetaCyc:HS04076-MONOMER.
ZFISH:HS04076-MONOMER.
ReactomeiR-HSA-156581. Methylation.
R-HSA-1614635. Sulfur amino acid metabolism.
R-HSA-196741. Cobalamin (Cbl, vitamin B12) transport and metabolism.
R-HSA-3359467. Defective MTRR causes methylmalonic aciduria and homocystinuria type cblE.
R-HSA-3359469. Defective MTR causes methylmalonic aciduria and homocystinuria type cblG.

Miscellaneous databases

ChiTaRSiMTR. human.
EvolutionaryTraceiQ99707.
GeneWikiiMethionine_synthase.
GenomeRNAii4548.
PROiQ99707.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116984.
CleanExiHS_MTR.
ExpressionAtlasiQ99707. baseline and differential.
GenevisibleiQ99707. HS.

Family and domain databases

CDDicd02069. methionine_synthase_B12_BD. 1 hit.
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.
IPR003726. HCY_dom.
IPR033706. Met_synthase_B12-bd.
IPR011822. MetH.
IPR000489. Pterin-binding_dom.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiMETH_HUMAN
AccessioniPrimary (citable) accession number: Q99707
Secondary accession number(s): A1L4N8
, A9Z1W4, B7ZLW7, B9EGF7, Q99713, Q99723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.