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Database: UniProt
Entry: A3YY11_9SYNE
LinkDB: A3YY11_9SYNE
Original site: A3YY11_9SYNE 
ID   A3YY11_9SYNE            Unreviewed;       256 AA.
AC   A3YY11;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Putative precorrin-4 c11-methyltransferase {ECO:0000313|EMBL:EAQ74978.1};
GN   ORFNames=WH5701_07849 {ECO:0000313|EMBL:EAQ74978.1};
OS   Synechococcus sp. WH 5701.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ74978.1, ECO:0000313|Proteomes:UP000002935};
RN   [1] {ECO:0000313|EMBL:EAQ74978.1, ECO:0000313|Proteomes:UP000002935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH5701 {ECO:0000313|Proteomes:UP000002935};
RA   Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) 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|RuleBase:RU003960}.
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:EAQ74978.1}.
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DR   EMBL; AANO01000005; EAQ74978.1; -; Genomic_DNA.
DR   RefSeq; WP_006170307.1; NZ_CH724159.1.
DR   AlphaFoldDB; A3YY11; -.
DR   eggNOG; COG2875; Bacteria.
DR   HOGENOM; CLU_011276_7_1_3; -.
DR   OrthoDB; 9815856at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002935; Unassembled WGS sequence.
DR   GO; GO:0046026; F:precorrin-4 C11-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11641; Precorrin-4_C11-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; IPR006362; Cbl_synth_CobM/CibF.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01465; cobM_cbiF; 1.
DR   PANTHER; PTHR45790:SF4; COBALT-PRECORRIN-4 C(11)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF00590; TP_methylase; 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:UP000002935};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          3..205
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   256 AA;  27502 MW;  E8796FA0A622D19A CRC64;
     MRIVGAGPGA IDLMTVRATR AVEAADVLVW TDSLVSPQIA ALAPQHCERI RTSTLTLEEV
     MELVVERARA GLRVVRLHDG DPCLYGALAE QICRLADAGL EVEVVPGLSA YQATAAALKA
     ELTIPGLVQT IVLSRAGGRT GVPERESLAH LASLRASLCL YLSARHVESV QQELLEHYAA
     DTPVAIGYRV SWPDQWLQVV PLEQMAAVSR ERQLIRTTLY VVSPALAAPE QARSRLYSAS
     HDHLFRAATA AGGSEG
//
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