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Database: UniProt
Entry: A0A1A5X3Z9_9BACL
LinkDB: A0A1A5X3Z9_9BACL
Original site: A0A1A5X3Z9_9BACL 
ID   A0A1A5X3Z9_9BACL        Unreviewed;       260 AA.
AC   A0A1A5X3Z9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Precorrin-4 C(11)-methyltransferase {ECO:0000313|EMBL:OBR48059.1};
DE            EC=2.1.1.133 {ECO:0000313|EMBL:UYZ12813.1};
GN   Name=cobM {ECO:0000313|EMBL:UYZ12813.1};
GN   ORFNames=A6764_16835 {ECO:0000313|EMBL:OBR48059.1}, A6764_18705
GN   {ECO:0000313|EMBL:UYZ12813.1};
OS   Brevibacillus sp. WF146.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=319501 {ECO:0000313|EMBL:OBR48059.1};
RN   [1] {ECO:0000313|EMBL:OBR48059.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF146 {ECO:0000313|EMBL:OBR48059.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:UYZ12813.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WF146 {ECO:0000313|EMBL:UYZ12813.1};
RA   Tang B., Tang X.-F., Zhu F., Li Y.;
RT   "Complete genome sequence of Brevibacillus thermoruber WF146.";
RL   Submitted (OCT-2022) 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, ECO:0000256|RuleBase:RU003960}.
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DR   EMBL; LXGJ01000256; OBR48059.1; -; Genomic_DNA.
DR   EMBL; CP109943; UYZ12813.1; -; Genomic_DNA.
DR   RefSeq; WP_035300771.1; NZ_LXGJ01000256.1.
DR   AlphaFoldDB; A0A1A5X3Z9; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000093585; Chromosome.
DR   GO; GO:0046026; F:precorrin-4 C11-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; cd11641; Precorrin-4_C11-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; IPR006362; Cbl_synth_CobM/CibF.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01465; cobM_cbiF; 1.
DR   PANTHER; PTHR45790:SF4; COBALT-PRECORRIN-4 C(11)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU003960};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093585};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          2..208
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   260 AA;  28201 MW;  4F6ACB1BDB955C15 CRC64;
     MKLYIVGAGP GDPDLITVKG LKLLQQADVV LYTDSLVSDE LAAKAKPGAE VLQSSGMALE
     EMVELMVDRV RQGKTVVRLH TGDPSVYGAT MEQIALLKRA GIDVEIVPGV SSVFAAAAAL
     GAELTIPELT QTLILTRAEG RTPVPEREKL RALAEHHCTI ALFLSATLTK KVVRELTEAG
     WSEDTPVAVV QRASWPDQVI VRTTLKHLDE EMGKHGIRSH AMILAGWALD PAIHEKSGQH
     RSKLYDKTFT HGYRKGVTEG
//
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