ID J2D8P3_9SPHN Unreviewed; 250 AA.
AC J2D8P3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Precorrin-6A synthase [deacetylating] {ECO:0000256|PIRNR:PIRNR036525};
DE EC=2.1.1.152 {ECO:0000256|PIRNR:PIRNR036525};
GN ORFNames=PMI04_00603 {ECO:0000313|EMBL:EJK86184.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK86184.1};
RN [1] {ECO:0000313|EMBL:EJK86184.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK86184.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJK86184.1}.
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DR EMBL; AJVL01000009; EJK86184.1; -; Genomic_DNA.
DR RefSeq; WP_007705565.1; NZ_CP124576.1.
DR AlphaFoldDB; J2D8P3; -.
DR STRING; 1144307.PMI04_00603; -.
DR PATRIC; fig|1144307.3.peg.564; -.
DR eggNOG; COG2243; Bacteria.
DR OrthoDB; 9787471at2; -.
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 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 4..222
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 250 AA; 27228 MW; A9664D9C6BBCEBCA CRC64;
MIDISLIGIG TGNPDHLTAE AVKAMNAANL ILLPRKGDAK SDLIDLRRDI CAAMLSPSVH
VVEFDLPVRA SGTPDYLNAV AAWHDAIAHI WAEQIRRHLP TGGRLALLIW GDPSLYDSSL
RIVERLSSIG MTTKVRVVPG ITSIQALTAA HALSLNQLGA PITITTGRLL RTHGWPDHAD
TLVVMLDEGC AFEAIPPDGI HIWWGAYLGM AQQVLVEGPL SKVGQTIKAV RADSRARHGW
IMDIYILRRR
//
