ID J0UB25_9BURK Unreviewed; 251 AA.
AC J0UB25;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Precorrin-2 C(20)-methyltransferase {ECO:0000256|PIRNR:PIRNR036427};
DE EC=2.1.1.130 {ECO:0000256|PIRNR:PIRNR036427};
GN ORFNames=PMI14_01987 {ECO:0000313|EMBL:EJE53387.1};
OS Acidovorax sp. CF316.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE53387.1, ECO:0000313|Proteomes:UP000004811};
RN [1] {ECO:0000313|EMBL:EJE53387.1, ECO:0000313|Proteomes:UP000004811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF316 {ECO:0000313|EMBL:EJE53387.1,
RC ECO:0000313|Proteomes:UP000004811};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- FUNCTION: Methylates precorrin-2 at the C-20 position to produce
CC precorrin-3A. {ECO:0000256|PIRNR:PIRNR036427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=precorrin-2 + S-adenosyl-L-methionine = H(+) + precorrin-3A +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:16841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58561, ChEBI:CHEBI:58827,
CC ChEBI:CHEBI:59789; EC=2.1.1.130;
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|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:EJE53387.1}.
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DR EMBL; AKJX01000094; EJE53387.1; -; Genomic_DNA.
DR AlphaFoldDB; J0UB25; -.
DR PATRIC; fig|1144317.3.peg.1677; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000004811; Unassembled WGS sequence.
DR GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:UniProtKB-EC.
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 InterPro; IPR001763; Rhodanese-like_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.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:EJE53387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004811};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJE53387.1}.
FT DOMAIN 31..68
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 251 AA; 27614 MW; FC62CBCC4B242EE0 CRC64;
MAVAQAAPGI VCVGLGPGDP ELMSVKAHRL VRSARYVAFF RKKGRPGKAR QVVDGLLAAE
ATEYPMEYPV TTELPVDSPE YVAQLAAFYD DWCTRLETLA RTEQVVVLCE GDPFLYGSFM
HLYTRLRERA AVRLEVVPGI PGMVGCWHAT GEPITWGDDV LSVMTGTLSE DELVRRMQTA
DALVVMKVGR NLPRIRRALQ RTGRLGAAWL VQNGTTASQQ VAKLTEVSDE ACPYFAIVLV
HGQGRRPEAA W
//
