ID A0A2A9FI61_9PSEU Unreviewed; 253 AA.
AC A0A2A9FI61;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Precorrin-6A synthase (Deacetylating) {ECO:0000313|EMBL:PFG50119.1};
GN ORFNames=ATK36_5324 {ECO:0000313|EMBL:PFG50119.1};
OS Amycolatopsis sulphurea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=76022 {ECO:0000313|EMBL:PFG50119.1, ECO:0000313|Proteomes:UP000243542};
RN [1] {ECO:0000313|EMBL:PFG50119.1, ECO:0000313|Proteomes:UP000243542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46092 {ECO:0000313|EMBL:PFG50119.1,
RC ECO:0000313|Proteomes:UP000243542};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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}.
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:PFG50119.1}.
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DR EMBL; PDJK01000002; PFG50119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9FI61; -.
DR Proteomes; UP000243542; Unassembled WGS sequence.
DR GO; GO:0043819; F:precorrin-6A synthase (deacetylating) activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11643; Precorrin-6A-synthase; 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; IPR012797; CobF.
DR NCBIfam; TIGR02434; CobF; 1.
DR PANTHER; PTHR43467; COBALT-PRECORRIN-2 C(20)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43467:SF1; PRECORRIN-6A SYNTHASE [DEACETYLATING]; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036525; CobF; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000243542};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..218
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 253 AA; 28762 MW; 89E5FF5B14098C2D CRC64;
MRRIYAIGIG AGDPEHLTVQ AIDRLNRVDV FFVLDKGEAK ADLVRLRQDI LDRFVTRPGY
RVVSAQDPDR DRTPADYRVA VADWHQLRTD VYERLIRDEL GEDETGAFLV WGDPSLYDST
IALIEAVLAR ETVEFDYEVV PGVSSVSALA ARHRTTMNQI GRAVHFTTGR RLSEGWPADA
DDVFVLLDAH TTFDRFADQG VWIYWGAYLG TPEEILVSGL LDAGLATRIR ELRAEARERN
GWIMDTYLLR RPR
//
