ID A0A1M6GTT6_9ACTN Unreviewed; 246 AA.
AC A0A1M6GTT6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Precorrin-6A synthase (Deacetylating) {ECO:0000313|EMBL:SHJ13361.1};
GN ORFNames=SAMN02745244_01792 {ECO:0000313|EMBL:SHJ13361.1};
OS Tessaracoccus bendigoensis DSM 12906.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1123357 {ECO:0000313|EMBL:SHJ13361.1, ECO:0000313|Proteomes:UP000184512};
RN [1] {ECO:0000313|EMBL:SHJ13361.1, ECO:0000313|Proteomes:UP000184512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12906 {ECO:0000313|EMBL:SHJ13361.1,
RC ECO:0000313|Proteomes:UP000184512};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQZG01000028; SHJ13361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6GTT6; -.
DR STRING; 1123357.SAMN02745244_01792; -.
DR OrthoDB; 9787471at2; -.
DR Proteomes; UP000184512; 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 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 SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000184512};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..219
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 246 AA; 26680 MW; 5FAA617F990E7B4A CRC64;
MSGVARKVFV IGLGPGGFGQ LTLDAVDAMN SVDVFLVADS DDNQSDQVWR RSELIRRNVK
RVHRVVTVLD PAHTQADDGE IDAARLAPYS QIMSGLPDDA TVGFLAWGDP AVYDSVLRVV
DELRGAIPMD VTVIPGVSAP QLLAAAHAIA LNRAGQSVHL TIGARLLSEY HPGLGDFVVL
DDADFTCQAL VAEFPDTELF WGAYLGTADQ VLASGPLRTV VPELQRVRQR LISQHSWIQD
IYLLRS
//