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Database: UniProt
Entry: T0Z419_9BACT
LinkDB: T0Z419_9BACT
Original site: T0Z419_9BACT 
ID   T0Z419_9BACT            Unreviewed;       266 AA.
AC   T0Z419;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=5-methyltetrahydrofolate-homocysteine methyltransferase {ECO:0000313|EMBL:EQD24355.1};
DE   Flags: Fragment;
GN   ORFNames=D084_Lepto4C00468G0001 {ECO:0000313|EMBL:EQD24355.1};
OS   Leptospirillum sp. Group IV 'UBA BS'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1260983 {ECO:0000313|EMBL:EQD24355.1, ECO:0000313|Proteomes:UP000017751};
RN   [1] {ECO:0000313|EMBL:EQD24355.1, ECO:0000313|Proteomes:UP000017751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23645189; DOI=10.1128/AEM.00202-13;
RA   Goltsman D.S., Dasari M., Thomas B.C., Shah M.B., VerBerkmoes N.C.,
RA   Hettich R.L., Banfield J.F.;
RT   "New group in the Leptospirillum clade: cultivation-independent community
RT   genomics, proteomics, and transcriptomics of the new species
RT   "Leptospirillum group IV UBA BS".";
RL   Appl. Environ. Microbiol. 79:5384-5393(2013).
CC   -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC       family. {ECO:0000256|ARBA:ARBA00010398}.
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:EQD24355.1}.
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DR   EMBL; AURA01000468; EQD24355.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0Z419; -.
DR   HOGENOM; CLU_070996_0_0_0; -.
DR   Proteomes; UP000017751; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   InterPro; IPR000489; Pterin-binding_dom.
DR   PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR   PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR   Pfam; PF00809; Pterin_bind; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EQD24355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017751};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EQD24355.1}.
FT   DOMAIN          1..216
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
FT   REGION          236..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         266
FT                   /evidence="ECO:0000313|EMBL:EQD24355.1"
SQ   SEQUENCE   266 AA;  28476 MW;  C2B8BAA28A2C055B CRC64;
     MAEARKEAAA GAHALDVNVG VPLVDEARMM EKAVTAIGNV VSLPLVIDSS FASALEAGLR
     LYPGRALVNS VNAEEERIEE VLPLIRRYGA AVIGLLSGED IPEKAADRIR NAEKILRAAE
     RFGLRPEDIV FDTLALTVSA VQEASRQTLE TIRILKTEWN ARTIVGLSNV SFGLPVRKTV
     HDTFLAMAIG SGLDGAICDP YDPLLHQTVA AASLFSGRDP ECRVFMEKAA TWTPLVPSNT
     AGTQTGMPAG GITPDHPLST PEKIER
//
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