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Database: UniProt
Entry: A0A0Q5URA5_9SPHN
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Original site: A0A0Q5URA5_9SPHN 
ID   A0A0Q5URA5_9SPHN        Unreviewed;       402 AA.
AC   A0A0Q5URA5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Precorrin-6Y methyltransferase {ECO:0000313|EMBL:KQS51400.1};
GN   ORFNames=ASG20_05060 {ECO:0000313|EMBL:KQS51400.1};
OS   Sphingomonas sp. Leaf198.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736299 {ECO:0000313|EMBL:KQS51400.1, ECO:0000313|Proteomes:UP000050871};
RN   [1] {ECO:0000313|Proteomes:UP000050871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA   Garrido-Oter R.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf198 {ECO:0000313|Proteomes:UP000050871};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQS51400.1}.
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DR   EMBL; LMPX01000001; KQS51400.1; -; Genomic_DNA.
DR   RefSeq; WP_056049325.1; NZ_LMPX01000001.1.
DR   AlphaFoldDB; A0A0Q5URA5; -.
DR   STRING; 1736299.ASG20_05060; -.
DR   OrthoDB; 9787825at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000050871; Unassembled WGS sequence.
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:KQS51400.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050871};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQS51400.1}.
FT   DOMAIN          10..196
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   402 AA;  42785 MW;  C6601D08DCEDDE5E CRC64;
     MVEARTVPWL TIVGINEDGP AGLSPASRTA IEDADLVTGA RRHLALLPDL RCDVAPWPIP
     FDDGIARLLE QRGRHVVLLV SGDPFWFGAG TTITRHLARD EWVAHPAVST FALAAARLGW
     PIDDTACLGL HAAPLTRLRP ILAPRRQVIV LVRDGAAVGQ LACYLDEQGF GASMLWILEA
     LGGPSERIRR STAATLDFAD IAHPVAVGVT VAGNGAVVPG AAGRPDHWFD HDGQITKRAV
     RALTLSALAP RPGETLWDIG AGSGSIGIEW LLSHASTSAV AFEADPVRAD RVRANATKLG
     VDRLRVINGR APEILEGLPS PDVVFVGGGL SNTLLDRLCA TLDAGTRLVA NAVTLESEIL
     LTQWHATKGG TLQRIELSDA APLGTRRGWR AHYPVVQWSV AL
//
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