ID S3Y5U3_9ACTN Unreviewed; 240 AA.
AC S3Y5U3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Cobalt-precorrin-2 C(20)-methyltransferase {ECO:0000256|PIRNR:PIRNR036427};
DE EC=2.1.1.151 {ECO:0000256|PIRNR:PIRNR036427};
GN ORFNames=HMPREF1531_01211 {ECO:0000313|EMBL:EPH03785.1};
OS Propionibacterium sp. oral taxon 192 str. F0372.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH03785.1, ECO:0000313|Proteomes:UP000014567};
RN [1] {ECO:0000313|EMBL:EPH03785.1, ECO:0000313|Proteomes:UP000014567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0372 {ECO:0000313|EMBL:EPH03785.1,
RC ECO:0000313|Proteomes:UP000014567};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methylates cobalt-precorrin-2 at the C-20 position to produce
CC cobalt-precorrin-3A in the anaerobic cobalamin biosynthesis pathway.
CC {ECO:0000256|PIRNR:PIRNR036427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-2 + S-adenosyl-L-methionine = Co-precorrin-3 +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17997,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:60053, ChEBI:CHEBI:60060; EC=2.1.1.151;
CC Evidence={ECO:0000256|PIRNR:PIRNR036427};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR036427}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|PIRNR:PIRNR036427}.
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:EPH03785.1}.
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DR EMBL; ATFL01000010; EPH03785.1; -; Genomic_DNA.
DR RefSeq; WP_016669011.1; NZ_KE340297.1.
DR AlphaFoldDB; S3Y5U3; -.
DR STRING; 1203605.HMPREF1531_01211; -.
DR PATRIC; fig|1203605.3.peg.1255; -.
DR eggNOG; COG2243; Bacteria.
DR HOGENOM; CLU_076014_1_1_11; -.
DR OrthoDB; 9804789at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000014567; Unassembled WGS sequence.
DR GO; GO:0043781; F:cobalt-factor II C20-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11645; Precorrin_2_C20_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; IPR012382; CobI/CbiL.
DR InterPro; IPR006364; CobI/CbiL/CobIJ_dom.
DR NCBIfam; TIGR01467; cobI_cbiL; 1.
DR PANTHER; PTHR43467; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43467:SF2; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036427; Precrrn-2_mtase; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EPH03785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014567};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPH03785.1}.
FT DOMAIN 2..216
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 240 AA; 24981 MW; D088571496A3B91C CRC64;
MRLVGIGVGP GDPELITVKA LNVLRTCDVI LVPATEASGD GAGRAEKIIV AACPEVGTRI
TRVPFSMADL SGVTKRRSEA WETSAKAAVE AFEAGATQVG FATIGDPSVY STFSYLAAGV
REHIAGLEVE VVPGIMAMQA LAAACLTPLV EGDETLALVP LKKGTEQLTA ISEVVDTCVV
YKAGRHVRKL AELVGDDPAV AGSNIGLPNQ VITPLSEVDE APYFTSVIWP PKRGGTGERI
//
