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Database: UniProt
Entry: A0A0N0E5L4_9PSED
LinkDB: A0A0N0E5L4_9PSED
Original site: A0A0N0E5L4_9PSED 
ID   A0A0N0E5L4_9PSED        Unreviewed;       400 AA.
AC   A0A0N0E5L4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Precorrin-6Y C5,15-methyltransferase (Decarboxylating) {ECO:0000313|EMBL:KPA92615.1};
DE            EC=2.1.1.132 {ECO:0000313|EMBL:KPA92615.1};
GN   ORFNames=PF66_01296 {ECO:0000313|EMBL:KPA92615.1};
OS   Pseudomonas fuscovaginae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA92615.1, ECO:0000313|Proteomes:UP000037931};
RN   [1] {ECO:0000313|EMBL:KPA92615.1, ECO:0000313|Proteomes:UP000037931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA92615.1,
RC   ECO:0000313|Proteomes:UP000037931};
RX   PubMed=26422147;
RA   Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA   Cruz C.V., Oliva R.;
RT   "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT   Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL   PLoS ONE 10:E0139256-E0139256(2015).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
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:KPA92615.1}.
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DR   EMBL; JSYZ01000003; KPA92615.1; -; Genomic_DNA.
DR   RefSeq; WP_054062175.1; NZ_JSYZ01000003.1.
DR   AlphaFoldDB; A0A0N0E5L4; -.
DR   STRING; 50340.PF66_01296; -.
DR   PATRIC; fig|50340.43.peg.4182; -.
DR   OrthoDB; 9787825at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000037931; Unassembled WGS sequence.
DR   GO; GO:0046025; F:precorrin-6Y C5,15-methyltransferase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd11644; Precorrin-6Y-MT; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR012818; CbiE.
DR   InterPro; IPR006365; Cbl_synth_CobL.
DR   InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR02467; CbiE; 1.
DR   NCBIfam; TIGR02469; CbiT; 1.
DR   PANTHER; PTHR43182; COBALT-PRECORRIN-6B C(15)-METHYLTRANSFERASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR43182:SF1; COBALT-PRECORRIN-7 C(5)-METHYLTRANSFERASE; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036428; CobL; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   4: Predicted;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KPA92615.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPA92615.1}.
FT   DOMAIN          5..186
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   400 AA;  42628 MW;  DA2824F2229460FE CRC64;
     MAPWLTVVGI GEDGFDGLGK NARQALLGAA RVFGGPRQLD LLPASVTAER QAWPSPFSLE
     PVLALRGTPV CVLASGDPML FGVGASLARQ VEPQEMHVLP APSAYSLAAA RLGWALQEVV
     CLSVVARPVA ALGAHLHTGL RLLVLSNDEH SPAAIVALLR ERGFGPSRVS VLEHLGGPLE
     RRIDGRARGW EEQPFARLNL VAIECQADPA TPRLSHIGGL PDSAFRHDGQ LTKRDVRAIT
     LARLAPVPGE LLWDVGAGSG SIGIEWMRAH PSCRTIAIEA DAGRQQLIEH NRDALGVPGL
     RLVRGNAPQA LDGLEQPDAI FIGGGVTVPG VVETCWARLK PGGRLVANAV TLQSELLLMN
     WRQSHGGELT RLHVAQAQPL GDFDTWRQAL PITLLDVVKP
//
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