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Database: UniProt
Entry: F3G681_PSESJ
LinkDB: F3G681_PSESJ
Original site: F3G681_PSESJ 
ID   F3G681_PSESJ            Unreviewed;       185 AA.
AC   F3G681;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Precorrin-4 C11-methyltransferase {ECO:0000313|EMBL:EGH42581.1};
DE   Flags: Fragment;
GN   ORFNames=PSYPI_09300 {ECO:0000313|EMBL:EGH42581.1};
OS   Pseudomonas syringae pv. pisi str. 1704B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH42581.1, ECO:0000313|Proteomes:UP000004986};
RN   [1] {ECO:0000313|EMBL:EGH42581.1, ECO:0000313|Proteomes:UP000004986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1704B {ECO:0000313|EMBL:EGH42581.1,
RC   ECO:0000313|Proteomes:UP000004986};
RX   PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA   Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA   Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT   "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT   genomics of 19 Pseudomonas syringae isolates.";
RL   PLoS Pathog. 7:E1002132-e1002132(2011).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953}.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005879}.
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:EGH42581.1}.
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DR   EMBL; AEAI01000466; EGH42581.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3G681; -.
DR   PATRIC; fig|629263.4.peg.1534; -.
DR   HOGENOM; CLU_1457472_0_0_6; -.
DR   Proteomes; UP000004986; Unassembled WGS sequence.
DR   GO; GO:0046026; F:precorrin-4 C11-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd11641; Precorrin-4_C11-MT; 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; IPR006362; Cbl_synth_CobM/CibF.
DR   PANTHER; PTHR45790:SF4; COBALT-PRECORRIN-4 C(11)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EGH42581.1};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGH42581.1}.
FT   DOMAIN          6..142
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGH42581.1"
SQ   SEQUENCE   185 AA;  20061 MW;  22F27F86A3AFB9EC CRC64;
     IKRVHAQGQD VARVHSGDPS LYGAIGEQIR HLRELGIPFE IIPGVTATAA CAALLGVELT
     LPDVSQSVIL TRYADKTSMP SGEELASLAS HRATMAIHLG VNNLQRIVEE LMPHYGADCP
     IAVVHRASWP DQDWAVGTLA DIQEKVQAKG FRRTALILVG RVLADDTFSE SSLYRAGHAH
     LFRPV
//
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