ID A0A2M8IU13_9RHOB Unreviewed; 250 AA.
AC A0A2M8IU13;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Precorrin-3B C(17)-methyltransferase {ECO:0000313|EMBL:PJE34002.1};
GN Name=cobJ {ECO:0000313|EMBL:PJE34002.1};
GN ORFNames=CVM52_24530 {ECO:0000313|EMBL:PJE34002.1};
OS Pseudooceanicola lipolyticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=2029104 {ECO:0000313|EMBL:PJE34002.1, ECO:0000313|Proteomes:UP000231553};
RN [1] {ECO:0000313|EMBL:PJE34002.1, ECO:0000313|Proteomes:UP000231553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=157 {ECO:0000313|EMBL:PJE34002.1,
RC ECO:0000313|Proteomes:UP000231553};
RX PubMed=29219804; DOI=10.1099/ijsem.0.002521;
RA Huang M.-M., Guo L.-L., Wu Y.-H., Lai Q.-L., Shao Z.-Z., Wang C.-S., Wu M.,
RA Xu X.-W.;
RT "Pseudooceanicola lipolyticus sp. nov., a marine alphaproteobacterium,
RT reclassification of Oceanicola flagellatus as Pseudooceanicola flagellatus
RT comb. nov. and emended description of the genus Pseudooceanicola.";
RL Int. J. Syst. Evol. Microbiol. 68:409-415(2018).
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:PJE34002.1}.
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DR EMBL; PGTB01000261; PJE34002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8IU13; -.
DR OrthoDB; 9772960at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000231553; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11646; Precorrin_3B_C17_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; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR NCBIfam; TIGR01466; cobJ_cbiH; 1.
DR PANTHER; PTHR47036; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR47036:SF1; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00590; TP_methylase; 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:PJE34002.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231553};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PJE34002.1}.
FT DOMAIN 5..212
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 250 AA; 26607 MW; 47E13C47B0FB1731 CRC64;
MTGALIIAGL GPGADALVTP QVAQALARAT DVVGYIPYVK RVAPRAGLTL HASDNRVELE
RARHALQMAA EGREVVVVSS GDPGVFAMAA AVFEALEDGP APWRDLDIQV LPGITAMLAA
AARAGAPLGH DFCAINLSDN LKPWDLIEKR LRLAAEADFA MAFYNPRSKS RPEGFARALD
VLRAACGDAR PVIFARAVST PEEELRCVPL PEARPEMADM RTVVLVGSSL TRVIERPQGP
LVYTPRSVPA
//