ID A0A0B4C7G3_9RHOB Unreviewed; 246 AA.
AC A0A0B4C7G3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Precorrin-6A synthase [deacetylating] {ECO:0000256|PIRNR:PIRNR036525};
DE EC=2.1.1.152 {ECO:0000256|PIRNR:PIRNR036525};
GN ORFNames=RA29_07000 {ECO:0000313|EMBL:KIC50441.1};
OS Tateyamaria sp. ANG-S1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tateyamaria.
OX NCBI_TaxID=1577905 {ECO:0000313|EMBL:KIC50441.1, ECO:0000313|Proteomes:UP000031171};
RN [1] {ECO:0000313|Proteomes:UP000031171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-S1 {ECO:0000313|Proteomes:UP000031171};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
CC -!- FUNCTION: Catalyzes the methylation of C-1 in precorrin-5 and the
CC subsequent extrusion of acetic acid from the resulting intermediate to
CC form cobalt-precorrin-6A. {ECO:0000256|PIRNR:PIRNR036525}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + precorrin-5 + S-adenosyl-L-methionine = acetate + 2 H(+)
CC + precorrin-6A + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:18261,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77871,
CC ChEBI:CHEBI:77872; EC=2.1.1.152;
CC Evidence={ECO:0000256|PIRNR:PIRNR036525};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
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:KIC50441.1}.
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DR EMBL; JWLL01000004; KIC50441.1; -; Genomic_DNA.
DR RefSeq; WP_039684378.1; NZ_JWLL01000004.1.
DR AlphaFoldDB; A0A0B4C7G3; -.
DR STRING; 1577905.RA29_07000; -.
DR OrthoDB; 9787471at2; -.
DR Proteomes; UP000031171; Unassembled WGS sequence.
DR GO; GO:0043819; F:precorrin-6A synthase (deacetylating) activity; IEA:UniProtKB-EC.
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 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR036525};
KW Reference proteome {ECO:0000313|Proteomes:UP000031171};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR036525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036525}.
FT DOMAIN 3..216
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 246 AA; 27391 MW; 57F394966F0E458D CRC64;
MELFLIGIGT GNPDHLTGEA RRVMAEADLF LVPHKGAGKS DLADLRTQII SDVRDDATVA
LFDMPVRDDS LPYIARVDAW HDEIARIWTE TMAQHPEARK VALLVWGDPS LYDSTLRIAA
RLEPKPEIRV VAGITSIQAL TAAHAIPLNT LNAPVTISTG RRLRDHGWPE GCETLVVMLD
GDCTFQTLDG DRFDIWWGAY LGMPEQILEH GRLADVSERI IARRAAARAA HGWIMDTYLL
RQLPEK
//