ID Q98L02_RHILO Unreviewed; 324 AA.
AC Q98L02;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=5-methyltetrahydrofolate S-homocysteine methyltransferase {ECO:0000313|EMBL:BAB48661.1};
GN OrderedLocusNames=mlr1243 {ECO:0000313|EMBL:BAB48661.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB48661.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB48661.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; BA000012; BAB48661.1; -; Genomic_DNA.
DR RefSeq; WP_010910015.1; NC_002678.2.
DR AlphaFoldDB; Q98L02; -.
DR GeneID; 66683576; -.
DR KEGG; mlo:mlr1243; -.
DR PATRIC; fig|266835.9.peg.1004; -.
DR eggNOG; COG1410; Bacteria.
DR HOGENOM; CLU_070996_0_0_5; -.
DR Proteomes; UP000000552; Chromosome.
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:BAB48661.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAB48661.1}.
FT DOMAIN 21..269
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT REGION 296..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 34280 MW; 32A599B5D986635B CRC64;
MTRTIVASAT REIIIGFDQP FCVIGERINP TGRKKLAAEM VAGNFETVIK DALEQAACGA
TMLDVNAGVT AVDPNATEPA LLVQTLEIVQ GLVDLPLSID SSVTAAIEAA LKVAKGRPLV
NSVTGEEEKL EAILPLIKKY NVPVVAISND ETGISMDPDV RFAVAKKIVQ RCADFGIPAH
DVVVDPLVMP IGALGDAGRQ VFALLRRLRE ELKVNTTCGL SNISFGLPHR HGINAAFIPM
VIGAGMTSAI MNPVRPQEME AVRGANVLNG TDENCTNWIR TYKDYKPAEG GHAVAAPTQV
NAPGDGAANG GRRRGGREAR MGRG
//
