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Database: UniProt
Entry: A0A1M6GTT6_9ACTN
LinkDB: A0A1M6GTT6_9ACTN
Original site: A0A1M6GTT6_9ACTN 
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
//
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