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Database: UniProt
Entry: S5XT14_PARAH
LinkDB: S5XT14_PARAH
Original site: S5XT14_PARAH 
ID   S5XT14_PARAH            Unreviewed;       263 AA.
AC   S5XT14;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Precorrin-4 C11-methyltransferase {ECO:0000313|EMBL:AGT08287.1};
DE            EC=2.1.1.133 {ECO:0000313|EMBL:AGT08287.1};
GN   ORFNames=JCM7686_1178 {ECO:0000313|EMBL:AGT08287.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT08287.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT08287.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT08287.1};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(2014).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879}.
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DR   EMBL; CP006650; AGT08287.1; -; Genomic_DNA.
DR   RefSeq; WP_020949925.1; NC_022041.1.
DR   AlphaFoldDB; S5XT14; -.
DR   STRING; 1367847.JCM7686_1178; -.
DR   KEGG; pami:JCM7686_1178; -.
DR   PATRIC; fig|1367847.3.peg.1146; -.
DR   eggNOG; COG2875; Bacteria.
DR   HOGENOM; CLU_011276_7_1_5; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000015480; Chromosome.
DR   GO; GO:0046026; F:precorrin-4 C11-methyltransferase activity; IEA:UniProtKB-EC.
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.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:AGT08287.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGT08287.1}.
FT   DOMAIN          2..209
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   263 AA;  27826 MW;  B0B7F689982A23C8 CRC64;
     MTVHFIGAGP GAPDLLTLRA ARLIAACPVC LYAGSLIPAE VLGHCPEGAR IVNTASLSLD
     EIMAEIARAH AEGHDIARLH SGDLSVWSAM GEQLRRLREL GIPYDVTPGV PSFAAAAAAL
     GAELTLPGQA QSVILTRTSG RATALPEGET LEAFAATGAT LAIHLSIHVS DEVQRRLIPY
     LRGDCPVAVV WRASWPDQQI ERGTLAELAT LAAKGSERTA LILVGRNLAE APDGFGESRL
     YAGDYDRRFR PVGAAPRFPE GRE
//
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