ID A0A418SKU5_9RHOB Unreviewed; 235 AA.
AC A0A418SKU5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Precorrin-2 C(20)-methyltransferase {ECO:0000313|EMBL:QPM91029.1};
DE EC=2.1.1.130 {ECO:0000313|EMBL:QPM91029.1};
GN Name=cobI {ECO:0000313|EMBL:QPM91029.1};
GN ORFNames=PSAL_022720 {ECO:0000313|EMBL:QPM91029.1};
OS Pseudooceanicola algae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1537215 {ECO:0000313|EMBL:QPM91029.1, ECO:0000313|Proteomes:UP000283786};
RN [1] {ECO:0000313|EMBL:QPM91029.1, ECO:0000313|Proteomes:UP000283786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lw-13e {ECO:0000313|EMBL:QPM91029.1,
RC ECO:0000313|Proteomes:UP000283786};
RA Poehlein A., Wolter L., Daniel R., Brinkhoff T.;
RT "Genome sequence of Rhodobacteraceae bacterium Lw-13e.";
RL Submitted (AUG-2020) 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|PIRNR:PIRNR036427,
CC ECO:0000256|RuleBase:RU003960}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP060436; QPM91029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418SKU5; -.
DR KEGG; palw:PSAL_022720; -.
DR OrthoDB; 9804789at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000283786; Chromosome.
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; IPR003043; Uropor_MeTrfase_CS.
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; 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:UP000283786};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 5..210
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 235 AA; 24888 MW; 44FCF1554A4699C4 CRC64;
MSNGTLYGVG LGPGDPGLIT LRAAELIRAA QVLAYPARPG EPSMARAIAA GLIPEGVEEI
VMEVPMTPAR APAQAAYDSG ADRIAEALEN GRDVVCLCEG DPLFYGSFMY LQARLAARFT
VQIVPGVTSV SAAAARAGRA LVARNQRLEV LPGPLPDDAL RARLREGADT IVILKVGRHL
RRIRALLGGM GLMKQALYIE RATLPGEVIL PLADAPGEAP YFSLILITKG EDPWL
//
