ID A0A0L6CXP7_9RHOB Unreviewed; 354 AA.
AC A0A0L6CXP7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase {ECO:0000313|EMBL:KNX42455.1};
DE EC=2.1.1.258 {ECO:0000313|EMBL:KNX42455.1};
GN Name=acsE {ECO:0000313|EMBL:KNX42455.1};
GN ORFNames=ROTO_09640 {ECO:0000313|EMBL:KNX42455.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX42455.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KNX42455.1}.
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DR EMBL; LGVV01000008; KNX42455.1; -; Genomic_DNA.
DR RefSeq; WP_050661896.1; NZ_LGVV01000008.1.
DR AlphaFoldDB; A0A0L6CXP7; -.
DR STRING; 74031.SAMN04488077_102114; -.
DR PATRIC; fig|74031.6.peg.987; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000037046; Unassembled WGS sequence.
DR GO; GO:0102036; F:methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase 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:KNX42455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037046};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNX42455.1}.
FT DOMAIN 21..273
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT REGION 327..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 37640 MW; 1E7A2A20D32BE87A CRC64;
MTRTIVESKT KTAVIGFDEP FCVIGERINP TGRKKLAAEL EAGDYSTVES DAIAQAAAGA
TVLDINAGVV YNSNPNPNET EPPLMTAIVE LVQGLVDLPL CIDSSVPAAL EAGLQAAHGR
PLLNSVTGEE DRLEYVLPLV KKYNVPVVAI SNDDTGISED PDVRFAVAKK IVERAADFGI
PAHDIVVDPL VMPIGAMGTA GQQVFTLVRR LREELGVNTT CGASNISFGL PNRHGINNAF
LPMAMGAGMT SAIMNPIALP VKQAEMEAKK AEIAAAGLIL PEDMDDETFC QLFGLGSMKP
RAGKEMEAIM AANFLTNNDP HGGNWIKFNK APPKPGEEVR TGGRAGSRSR RRRA
//
