ID Q164M4_ROSDO Unreviewed; 360 AA.
AC Q164M4;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=5-methyltetrahydrofolate--homocysteine methyltransferase, putative {ECO:0000313|EMBL:ABG32569.1};
DE EC=2.1.1.13 {ECO:0000313|EMBL:ABG32569.1};
GN Name=metH {ECO:0000313|EMBL:ABG32569.1};
GN OrderedLocusNames=RD1_3057 {ECO:0000313|EMBL:ABG32569.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG32569.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG32569.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; CP000362; ABG32569.1; -; Genomic_DNA.
DR RefSeq; WP_011569185.1; NZ_FOOO01000002.1.
DR AlphaFoldDB; Q164M4; -.
DR STRING; 375451.RD1_3057; -.
DR KEGG; rde:RD1_3057; -.
DR eggNOG; COG1410; Bacteria.
DR HOGENOM; CLU_070996_0_0_5; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000007029; Chromosome.
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 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:ABG32569.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007029};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABG32569.1}.
FT DOMAIN 21..279
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT REGION 336..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 360 AA; 38400 MW; 2B31BC2EE955F46F CRC64;
MTKTIVESKT KTAIIGFDQP FCVIGERINP TGRKKLALEL EAGDFSTVEA DAMAQVAAGA
TVLDINSGAV FSNKMAEDTR YADNNFVEPP LMRELVLRVQ AIVDVPLCID SSVPGALESG
LEAAEGRPLL NSVTGEEERL EVVLPLVKKY NVPVVAISND DTGISEDPDV RFAVAKKIVE
RAADFGIPAH DIVVDPLVMP IGAMATAGHQ VFTLVRRLRE ELGVNTTCGA SNISFGLPNR
HGINNAFLPM AMGAGMTSAI MNPVALPVSA ARIEAKKMEL AAAGVVFPED MDLETFCQLT
GLGSTRPRPG KEMEAIRAAN FLTNNDPHGG AWIAFNKEAP KPGQEGRGRA ARTGGRRRRA
//
