ID R1EEN9_EMIHU Unreviewed; 1825 AA.
AC R1EEN9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=methionine synthase {ECO:0000256|ARBA:ARBA00012032};
DE EC=2.1.1.13 {ECO:0000256|ARBA:ARBA00012032};
DE AltName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase {ECO:0000256|ARBA:ARBA00031040};
DE AltName: Full=Vitamin-B12 dependent methionine synthase {ECO:0000256|ARBA:ARBA00030163};
GN ORFNames=EMIHUDRAFT_242970 {ECO:0000313|EMBL:EOD19344.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD19344.1};
RN [1] {ECO:0000313|EMBL:EOD19344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD19344.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD19344}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|PROSITE-ProRule:PRU00333};
CC -!- COFACTOR:
CC Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115;
CC Evidence={ECO:0000256|ARBA:ARBA00001956};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005178}.
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; KB866267; EOD19344.1; -; Genomic_DNA.
DR RefSeq; XP_005771773.1; XM_005771716.1.
DR STRING; 2903.R1EEN9; -.
DR PaxDb; 2903-EOD19344; -.
DR EnsemblProtists; EOD19344; EOD19344; EMIHUDRAFT_242970.
DR GeneID; 17264890; -.
DR KEGG; ehx:EMIHUDRAFT_242970; -.
DR eggNOG; KOG1579; Eukaryota.
DR eggNOG; KOG3664; Eukaryota.
DR HOGENOM; CLU_237516_0_0_1; -.
DR UniPathway; UPA00051; UER00081.
DR Proteomes; UP000013827; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008705; F:methionine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR Pfam; PF02460; Patched; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR Pfam; PF02574; S-methyl_trans; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR PROSITE; PS50970; HCY; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00333}.
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 671..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 701..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 731..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1022..1345
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT DOMAIN 1376..1647
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT BINDING 1267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 1330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 1331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 1825 AA; 198274 MW; EAF7F94ED5C25A38 CRC64;
MSGGESGEGA AVDITKEFFF SDSGIRSGRA SCGCASLAIS ATVTVLLAVV ALVAGNFSIA
ADNAGWYSRG TTLADRHVQL LRLFDWEWTG SEYTGCFPSI SADCWAQEPR RLSEEKCKKT
RSSDLTVIYR AKQSDADLLS PELLRQVCEL ESEAIRVLRA GACQPPSSGC SAVRGGECLA
PVSVVSLLRD SLGWELACAD LAADPATVGL AEALGLVGYD YTADSPSTRT LAAVFPLVRD
SALDFLLEVH HAGTLRLASA DVDTAYGMWR RDDFRDAVRD EVLFSDMALV YGSLVVSLVC
VLAYTRSLFL SVVGLLQVCF SFPLAFFCYS IVCRLDFFPF LNFLGLFVIM GIGVDDLFVV
VDKWSQAARS LPPGSDHRWL QRAPSSRRAR CLLSLLDFSR CSSRPPQEAA APRARVLERL
MSGPMHIAVH RGRFVLLVLF FAALGLCVWQ VANISPPSST AVQLLPESHV VERYETWKQD
FAEEDSSEMF VVWGLTPGDT GDHNNPELVT DLLADLDWDP SSREAQRWLL DFCNATASDP
AAPRATDIGC PLRDMDGWLV DSAAAGQPRC GGASRLPVPP DAFHPCVEEY LSSEDRYSWY
RGMRTYRGRL VALVASYKVV INFDSSYEQV RDTVDEWEGW MDTQNKGAPD GVRGGFFTSA
RVHWWDTNRS MLLGAYYSIG AALAVVFVVV LLATLNPLTT VYATVSVGTV LLLVIGTVLG
MGWELGFLEG ICFAILIGLS CDFVLHMAHA YTSADQPTRE LKSRDALARM GPPVFAAAMT
TLSTGLVMFG CTFVFFFQFG TILVLTMLYS ILTSLFFFLP LTNAAGPTGR CCSLAPLCAK
GRASGGADKE ASTQQARAAE PETGQIPPQL SLFVDTIPMV DSDAVAEAVR KEIERQMANP
DYDTLTTEEL KEAIGALKGR LESALSALTR KMDPSASPAS AAPAMGASAA ASASACAALS
GACARGCCVS TSSSQASTRA ARLGLEGATP GATPAELLSA PKSEGEFPDL PWGTPVDADK
VRDYLTNAMQ ERVLVLDGAM GTTIQQYKFT EQHFRGDKWP DWHIDLKGNN DLLVFTQPDT
IRDIHRRYFL AGADIVETNT FSGTTIAQAD YDMEDIVYEL NKVASELAVE AAKEVTALEP
HKPRLVAGAI GPTNRTLSIS PSVEDPGARN CDWDGVVAAY KQQTLGLIDG GCHILMVETI
FDTLNAKAAL FAIDEVYDER PDLPKLPIII SGASASRRSG RTLSGQTTEA FYVSVQHAKP
LVIGLNCALG AAGMVPFMQA MSEVAECFMQ CYPNAGLPNA MGGYDMTPDQ FAESVKPFCE
LGLTNMLGGC CGTTPEHIGA LAKMLERERF KPRVRPTKPQ HMWLSGLEAI DATGSYLNIG
ERCNIAGSLK FKKLILNGDY EKGLEIAKAQ AEGGAQVIDV NMDEGLLDGE FAMKKFLNML
IPEPDISRLP ICVDSSKFHV AEAGLKCCQG KCIFNSISLK EGEDEFIKKG KLVKRYGAAV
VVMAFDEEGQ AATYEDKIRI CKRAYDILVS DKASRRGGRY KTGRCKNHKC WREAIRFVAV
SQEGAGAFLN AIPMRDDMKM ETWAMRITVQ RRLGLPLDVA CQAVEAGKKA PNGKPHEELG
DAAMVNPRAK HATRHKYLLK RLVKTLRSAW GMLIEMEPTA HLSYSNPKQP DVAAANIGKG
HVRLVGDLKL TSSLACKGGD RLGWKGAFVA FGNTERALLD LGEYRFAREK NCDLRLLDFE
TFGGFGDGVR RILRQAADQL SNKLSHAQHL DEVTWTTKNW HGLQMQRLSV VLHTAVAWQT
VNELACGDSG IVHGAKCIAV LNGVA
//
