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Database: UniProt
Entry: A0A1Z3HM49_9CYAN
LinkDB: A0A1Z3HM49_9CYAN
Original site: A0A1Z3HM49_9CYAN 
ID   A0A1Z3HM49_9CYAN        Unreviewed;       208 AA.
AC   A0A1Z3HM49;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Precorrin-2 C(20)-methyltransferase {ECO:0000313|EMBL:ASC71360.1};
DE            EC=2.1.1.130 {ECO:0000313|EMBL:ASC71360.1};
GN   Name=cobI {ECO:0000313|EMBL:ASC71360.1};
GN   ORFNames=XM38_023120 {ECO:0000313|EMBL:ASC71360.1};
OS   Halomicronema hongdechloris C2206.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC   Halomicronema.
OX   NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC71360.1, ECO:0000313|Proteomes:UP000191901};
RN   [1] {ECO:0000313|EMBL:ASC71360.1, ECO:0000313|Proteomes:UP000191901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2206 {ECO:0000313|EMBL:ASC71360.1,
RC   ECO:0000313|Proteomes:UP000191901};
RX   PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA   Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA   Scheer H., Willows R.D., Chen M.;
RT   "Characterization of red-shifted phycobilisomes isolated from the
RT   chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL   Biochim. Biophys. Acta 1857:107-114(2016).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|PIRNR:PIRNR036427}.
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DR   EMBL; CP021983; ASC71360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z3HM49; -.
DR   KEGG; hhg:XM38_023120; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000191901; 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   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:ASC71360.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191901};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ASC71360.1}.
FT   DOMAIN          16..182
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   208 AA;  23205 MW;  8596204721F9FEE0 CRC64;
     MVAFPAGHDG LGVAQRTLMP WLRSEQQQLP LSFSFSQDRG QRQSAWQEAA AQVWGYLRRG
     DDVVFASEGD VSFYSTFTYL AQTLLTWHPQ VSVEVVPGVC SPLATAAVLG IPLTIQSQRL
     AVLPALYRVA ELERVLDWAE AVVLMKVSSV YPQVWSVLQQ RGLLSCSYVV QHVTWPDQLI
     YTDLQHHPNL ELSYFSVMII QVAANSLG
//
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