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Database: UniProt
Entry: G5J950_CROWT
LinkDB: G5J950_CROWT
Original site: G5J950_CROWT 
ID   G5J950_CROWT            Unreviewed;       497 AA.
AC   G5J950;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase {ECO:0000256|ARBA:ARBA00012034};
DE            EC=2.1.1.14 {ECO:0000256|ARBA:ARBA00012034};
DE   Flags: Fragment;
GN   ORFNames=CWATWH0003_3967a5 {ECO:0000313|EMBL:EHJ11258.1};
OS   Crocosphaera watsonii WH 0003.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ11258.1, ECO:0000313|Proteomes:UP000003477};
RN   [1] {ECO:0000313|EMBL:EHJ11258.1, ECO:0000313|Proteomes:UP000003477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ11258.1,
RC   ECO:0000313|Proteomes:UP000003477};
RX   PubMed=22232617;
RA   Bench S.R., Ilikchyan I.N., Tripp H.J., Zehr J.P.;
RT   "Two Strains of Crocosphaera watsonii with Highly Conserved Genomes are
RT   Distinguished by Strain-Specific Features.";
RL   Front. Microbiol. 2:261-261(2011).
CC   -!- FUNCTION: Catalyzes the transfer of a methyl group from 5-
CC       methyltetrahydrofolate to homocysteine resulting in methionine
CC       formation. {ECO:0000256|ARBA:ARBA00002777}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004681}.
CC   -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00009553}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHJ11258.1}.
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DR   EMBL; AESD01000606; EHJ11258.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5J950; -.
DR   UniPathway; UPA00051; UER00082.
DR   Proteomes; UP000003477; Unassembled WGS sequence.
DR   GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd03312; CIMS_N_terminal_like; 1.
DR   Gene3D; 3.20.20.210; -; 2.
DR   InterPro; IPR013215; Cbl-indep_Met_Synth_N.
DR   InterPro; IPR002629; Met_Synth_C/arc.
DR   InterPro; IPR038071; UROD/MetE-like_sf.
DR   PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR30519:SF0; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1.
DR   Pfam; PF08267; Meth_synt_1; 1.
DR   Pfam; PF01717; Meth_synt_2; 1.
DR   SUPFAM; SSF51726; UROD/MetE-like; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EHJ11258.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EHJ11258.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..333
FT                   /note="Cobalamin-independent methionine synthase MetE N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08267"
FT   DOMAIN          450..496
FT                   /note="Cobalamin-independent methionine synthase MetE C-
FT                   terminal/archaeal"
FT                   /evidence="ECO:0000259|Pfam:PF01717"
FT   NON_TER         497
FT                   /evidence="ECO:0000313|EMBL:EHJ11258.1"
SQ   SEQUENCE   497 AA;  55583 MW;  EEE669A7C7B052E7 CRC64;
     MNSIKTHSLG YPRIGAKREL KRATEAYWKG DLTLEELLAT GKTIRETNWK KQESAGIGLI
     PINDFSFYDQ MLDMSCLLGN VPARFKWTGG KTDVDTVFTV ARGTQGGVSL VEEEKDCQTG
     KVSTFASEMT KWFDTNYHYI VPEFRSDTTF KLSSDKIFEE FAEAKALGIN GKPVLIGPVT
     YLSLGKIQGT NNPDFDPFSL LDNLVDVYEE IIGKLAAAGA EWIQLDEPIF STDLSKEQLN
     ALKKSYDRLQ AAKGTAKILV TTYFGGVREN LGSYLSLPVD ALHFDFVRGA EDVETVLANF
     PSDKILSVGI VEGRNIWKNN YDRSLEVLQK ATAAVGADRL WVAPSCSLLH SPVTLENERK
     IDEELKSWMA FANEKLQEVV ELRQLLDGTG DEKALQANRE AIKARATSQR IHNEAVKTRL
     AGVGDRDFHR ASEFTVRQGK QQEKLQLPEF PTTTIGSFPQ TKEIRKARAQ WKKGAMSDAD
     YDQFLKTETA KCVTFQD
//
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