ID A0A0C1GXT1_9RHOB Unreviewed; 242 AA.
AC A0A0C1GXT1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Precorrin-2 C20-methyltransferase {ECO:0000313|EMBL:KIC43983.1};
DE EC=2.1.1.130 {ECO:0000313|EMBL:KIC43983.1};
GN ORFNames=RA28_13310 {ECO:0000313|EMBL:KIC43983.1};
OS Ruegeria sp. ANG-S4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC43983.1, ECO:0000313|Proteomes:UP000031326};
RN [1] {ECO:0000313|Proteomes:UP000031326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
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:KIC43983.1}.
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DR EMBL; JWLK01000005; KIC43983.1; -; Genomic_DNA.
DR RefSeq; WP_039529703.1; NZ_JWLK01000005.1.
DR AlphaFoldDB; A0A0C1GXT1; -.
DR STRING; 1577904.RA28_13310; -.
DR OrthoDB; 9804789at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000031326; 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 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:KIC43983.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031326};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIC43983.1}.
FT DOMAIN 5..219
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 242 AA; 26937 MW; 65F5C7393D7EA74A CRC64;
MSSGTVYGVG LGPGDPDLMS VRADRLLRNA RHVAYFRKHG RSGQARQIVN GMMPEGAVEF
PMEYPVTTEI PLDDPRYNQM LSTFYEDCAQ HLKTLAETGQ DVVVLCEGDP FFYGSFMHLY
NRLRDVVNVD VVPAITGMSG AWTATGDPIT WGDDVLTVLA GTLPEEDLAK RMAQTDALVV
MKIGRNFNKV KRALQSSGLY DRAWIVEYAQ MPNQRVCKLT ENCDGITPYF SIIIVHGQGR
RP
//