ID A0A225NH74_9RHOB Unreviewed; 246 AA.
AC A0A225NH74;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Precorrin-6A synthase [deacetylating] {ECO:0000256|PIRNR:PIRNR036525};
DE EC=2.1.1.152 {ECO:0000256|PIRNR:PIRNR036525};
GN ORFNames=ATO3_14780 {ECO:0000313|EMBL:OWU72946.1};
OS Marinibacterium profundimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marinibacterium.
OX NCBI_TaxID=1679460 {ECO:0000313|EMBL:OWU72946.1, ECO:0000313|Proteomes:UP000215377};
RN [1] {ECO:0000313|EMBL:OWU72946.1, ECO:0000313|Proteomes:UP000215377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-22F33 {ECO:0000313|EMBL:OWU72946.1,
RC ECO:0000313|Proteomes:UP000215377};
RA Lai Q., Li G., Shao Z.;
RT "Oceanicola sp. 22II1-22F33 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:OWU72946.1}.
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DR EMBL; AQQR01000005; OWU72946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225NH74; -.
DR OrthoDB; 9787471at2; -.
DR Proteomes; UP000215377; 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:UP000215377};
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..218
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 246 AA; 26632 MW; EC03C68BBA937A68 CRC64;
MITLHLIGIG TGNPDHVTME ARHAIAGADL VLVPEKGDGK SDLADLRRQI VAQVCDAPPV
IEGFGMPVRD PALPYLERVE RWHDAIAARW SEAIARHPQA RDVALLVWGD PSLYDSTLRI
AARLDPQPRL RVVAGITSLQ ALTAAHAIPL NTVNGPVVIT TGRQLRDHGW PEGAETVAVM
LDGACSFDVL EPDGIAIWWG AFLGMENQIL EAGPLAEAGP RIVAARARAR EAHGWIMDIY
LLRRSG
//
