ID B1ANE3_HUMAN Unreviewed; 819 AA.
AC B1ANE3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|Ensembl:ENSP00000355535.3};
DE Flags: Fragment;
GN Name=MTR {ECO:0000313|Ensembl:ENSP00000355535.3};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000355535.3, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000355535.3, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H.,
RA Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C.,
RA Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R.,
RA Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.,
RA Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.,
RA Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R.,
RA Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D.,
RA Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A.,
RA Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S.,
RA Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A.,
RA Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S.,
RA Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A.,
RA Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L.,
RA Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z.,
RA Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C.,
RA Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M.,
RA Langford C.F., Pandian R.D., Porter K.M., Prigmore E.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [3] {ECO:0000313|Ensembl:ENSP00000355535.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC Evidence={ECO:0000256|PIRSR:PIRSR000381-1};
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; AL359185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; B1ANE3; -.
DR SMR; B1ANE3; -.
DR MassIVE; B1ANE3; -.
DR MaxQB; B1ANE3; -.
DR PeptideAtlas; B1ANE3; -.
DR ProteomicsDB; 3251; -.
DR Antibodypedia; 20817; 175 antibodies from 30 providers.
DR Ensembl; ENST00000366576.3; ENSP00000355535.3; ENSG00000116984.15.
DR UCSC; uc057qqm.1; human.
DR HGNC; HGNC:7468; MTR.
DR VEuPathDB; HostDB:ENSG00000116984; -.
DR GeneTree; ENSGT00420000029824; -.
DR HOGENOM; CLU_004914_2_0_1; -.
DR ChiTaRS; MTR; human.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000116984; Expressed in caput epididymis and 216 other cell types or tissues.
DR ExpressionAtlas; B1ANE3; baseline and differential.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0008705; F:methionine synthase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR CDD; cd02069; methionine_synthase_B12_BD; 1.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 1.10.288.10; Cobalamin-dependent Methionine Synthase, domain 2; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 2.
DR Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR Gene3D; 3.10.196.10; Vitamin B12-dependent methionine synthase, activation domain; 1.
DR InterPro; IPR003759; Cbl-bd_cap.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR033706; Met_synthase_B12-bd.
DR InterPro; IPR011822; MetH.
DR InterPro; IPR036594; Meth_synthase_dom.
DR InterPro; IPR000489; Pterin-binding_dom.
DR InterPro; IPR004223; VitB12-dep_Met_synth_activ_dom.
DR InterPro; IPR037010; VitB12-dep_Met_synth_activ_sf.
DR NCBIfam; TIGR02082; metH; 1.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF02607; B12-binding_2; 1.
DR Pfam; PF02965; Met_synt_B12; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR PIRSF; PIRSF000381; MetH; 2.
DR SMART; SM01018; B12-binding_2; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF56507; Methionine synthase activation domain-like; 1.
DR SUPFAM; SSF47644; Methionine synthase domain; 1.
DR PROSITE; PS50974; ADOMET_ACTIVATION; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51337; B12_BINDING_NTER; 1.
PE 1: Evidence at protein level;
KW Cobalamin {ECO:0000256|PIRSR:PIRSR000381-1};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000381-1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00346};
KW Proteomics identification {ECO:0007829|EPD:B1ANE3,
KW ECO:0007829|MaxQB:B1ANE3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR000381-2};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00346}.
FT DOMAIN 216..313
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 326..461
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
FT DOMAIN 477..819
FT /note="AdoMet activation"
FT /evidence="ECO:0000259|PROSITE:PS50974"
FT BINDING 263
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 336..340
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 339
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /ligand_part="Co"
FT /ligand_part_id="ChEBI:CHEBI:27638"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-1"
FT BINDING 384
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 388
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 440
FT /ligand="methylcob(III)alamin"
FT /ligand_id="ChEBI:CHEBI:28115"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 528
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 726
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT BINDING 781..782
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000381-2"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000355535.3"
SQ SEQUENCE 819 AA; 91780 MW; 412970EB2FA276A1 CRC64;
GMLDGPSAMT RFCNLIASEP DIAKVPLCID SSNFAVIEAG LKCCQGKCIV NSISLKEGEA
TETDTKIRVC TRAYHLLVKK LGFNPNDIIF DPNILTIGTG MEEHNLYAIN FIHATKVIKE
TLPGARISGG LSNLSFSFRG MEAIREAMHG VFLYHAIKSG MDMGIVNAGN LPVYDDIHKE
LLQLCEDLIW NKDPEATEKL LRYAQTQGTG GKKVIQTDEW RNGPVEERLE YALVKGIEKH
IIEDTEEARL NQKKYPRPLN IIEGPLMNGM KIVGDLFGAG KMFLPQVIKS ARVMKKAVGH
LIPFMEKERE ETRVLNGTVE EEDPYQGTIV LATVKGDVHD IGKNIVGVVL GCNNFRVIDL
GVMTPCDKIL KAALDHKADI IGLSGLITPS LDEMIFVAKE MERLAIRIPL LIGGATTSKT
HTAVKIAPRY SAPVIHVLDA SKSVVVCSQL LDENLKDEYF EEIMEEYEDI RQDHYESLKE
RRYLPLSQAR KSGFQMDWLS EPHPVKPTFI GTQVFEDYDL QKLVDYIDWK PFFDVWQLRG
KYPNRGFPKI FNDKTVGGEA RKVYDDAHNM LNTLISQKKL RARGVVGFWP AQSIQDDIHL
YAEAAVPQAA EPIATFYGLR QQAEKDSAST EPYYCLSDFI APLHSGIRDY LGLFAVACFG
VEELSKAYED DGDDYSSIMV KALGDRLAEA FAEELHERVR RELWAYCGSE QLDVADLRRL
RYKGIRPAPG YPSQPDHTEK LTMWRLADIE QSTGIRLTES LAMAPASAVS GLYFSNLKSK
YFAVGKISKD QVEDYALRKN ISVAEVEKWL GPILGYDTD
//
