ID   PIGF_SERS3              Reviewed;         348 AA.
AC   Q5W266;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=S-adenosyl-L-methionine-dependent methyl transferase PigF {ECO:0000303|PubMed:15853884};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020, ECO:0000305|PubMed:15853884};
GN   Name=pigF {ECO:0000303|PubMed:15528645};
OS   Serratia sp. (strain ATCC 39006).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia; unclassified Serratia.
OX   NCBI_TaxID=104623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=15528645; DOI=10.1099/mic.0.27222-0;
RA   Harris A.K., Williamson N.R., Slater H., Cox A., Abbasi S., Foulds I.,
RA   Simonsen H.T., Leeper F.J., Salmond G.P.;
RT   "The Serratia gene cluster encoding biosynthesis of the red antibiotic,
RT   prodigiosin, shows species- and strain-dependent genome context
RT   variation.";
RL   Microbiology 150:3547-3560(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RC   STRAIN=ATCC 39006 / SC 11482;
RX   PubMed=15853884; DOI=10.1111/j.1365-2958.2005.04602.x;
RA   Williamson N.R., Simonsen H.T., Ahmed R.A., Goldet G., Slater H.,
RA   Woodley L., Leeper F.J., Salmond G.P.;
RT   "Biosynthesis of the red antibiotic, prodigiosin, in Serratia:
RT   identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway,
RT   definition of the terminal condensing enzyme, and implications for
RT   undecylprodigiosin biosynthesis in Streptomyces.";
RL   Mol. Microbiol. 56:971-989(2005).
CC   -!- FUNCTION: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-
CC       carbaldehyde (MBC), one of the terminal products involved in the
CC       biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the
CC       transfer of a methyl group from S-adenosyl-L-methionine (SAM) to the
CC       hydroxyl group of 4-hydroxy-2,2'-bipyrrole-5-carbaldehyde (HBC) to
CC       yield 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC).
CC       {ECO:0000269|PubMed:15853884}.
CC   -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC       {ECO:0000305|PubMed:15853884}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an orange phenotype
CC       and produce norprodigiosin. {ECO:0000269|PubMed:15853884}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR   EMBL; AJ833001; CAH55634.1; -; Genomic_DNA.
DR   RefSeq; WP_021014644.1; NZ_CP025085.1.
DR   AlphaFoldDB; Q5W266; -.
DR   SMR; Q5W266; -.
DR   STRING; 104623.Ser39006_01374; -.
DR   KEGG; ag:CAH55634; -.
DR   eggNOG; COG1414; Bacteria.
DR   eggNOG; COG4123; Bacteria.
DR   OrthoDB; 1213908at2; -.
DR   UniPathway; UPA01072; -.
DR   GO; GO:0008171; F:O-methyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR031725; ASMT_dimerisation.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11746; PTHR11746; 1.
DR   Pfam; PF16864; Dimerisation2; 1.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..348
FT                   /note="S-adenosyl-L-methionine-dependent methyl transferase
FT                   PigF"
FT                   /id="PRO_0000436243"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   348 AA;  38942 MW;  1C9B4FAB0B6A771B CRC64;
     MTLTKQDAVN QMMGFFQSKT LITALSLKLF DHLRDQDRNA KQMAALLNCP LRSSEQLLIA
     LQAMGYLEKQ DGLYHLPQEH RAFLVSDEPQ WLGWLGRHID TFLYPLWGEL KAAVENDTHQ
     RQTVFGDDRS WFDILYQNPD DVTDFQEFLG KFAAPFIDGF IQDYDFSQHQ AFLDIGSGIG
     SLPIAVANAY SGVNLAICEL PQTSTFLRDK LVQQGYGQRI QVLEGDVISG DLPIGDYDLI
     HLGWMLHDYA PETQLIILKN IYDAMPVGGR FIASETPLNA DKSGPEFTAL LSLNMLVSTD
     GGIESSPQEY LSRFHQAGFS NARIMDISGP RTLIVGEKTT HNNGSSQC