ID A8L754_FRASN Unreviewed; 301 AA.
AC A8L754;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Precorrin-2 C20-methyltransferase {ECO:0000313|EMBL:ABW13545.1};
GN ORFNames=Franean1_4161 {ECO:0000313|EMBL:ABW13545.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW13545.1};
RN [1] {ECO:0000313|EMBL:ABW13545.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW13545.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005879}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000820; ABW13545.1; -; Genomic_DNA.
DR AlphaFoldDB; A8L754; -.
DR STRING; 298653.Franean1_4161; -.
DR KEGG; fre:Franean1_4161; -.
DR eggNOG; COG2243; Bacteria.
DR HOGENOM; CLU_076014_1_1_11; -.
DR GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11645; Precorrin_2_C20_MT; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR012382; CobI/CbiL.
DR PANTHER; PTHR43467; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43467:SF2; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR Pfam; PF00590; TP_methylase; 2.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 2.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..39
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 148..274
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 40..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 30185 MW; D89B1523D3D469AD CRC64;
MSGTVNPRLV GVGVGPGDPD LVTYRAVRVL REATVVFVPV SDGHGPYGPA PGSPSPTDRP
GTATGVGVGP PGRAEMTVRA HVDHDRIVTL PFRMAGDADY LGPARVVAAA LRGETTGTAD
GVPDAGPPGT LAGPATAPDT GPGSGSGSGI TVAFATIGDP NLYSTFTALA AAVRTLLPDV
ELDTVPGITA MQDLAARSGT VLAHGAETLA LLPLTAGVEA YRSAVAGFDT VVAYKGGRAL
PAVRGVLADA ARLDGPAGHA VYGAALGLPE QDIRPAADLE PGETGPYLST VLATRRARWP
R
//
