ID   PAPM_STRPR              Reviewed;         292 AA.
AC   P72542;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=4-amino-L-phenylalanine/4-methylamino-L-phenylalanine methyltransferase {ECO:0000305};
DE            Short=PAPA/MMPAPA methyltransferase {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000269|PubMed:9044253};
DE   AltName: Full=SAM:PAPA/MMPAPA N-methyltransferase {ECO:0000305};
GN   Name=papM {ECO:0000303|PubMed:9044253};
OS   Streptomyces pristinaespiralis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=38300;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=SP92;
RX   PubMed=9044253; DOI=10.1046/j.1365-2958.1997.2031574.x;
RA   Blanc V., Gil P., Bamas-Jacques N., Lorenzon S., Zagorec M.,
RA   Schleuniger J., Bisch D., Blanche F., Debussche L., Crouzet J., Thibaut D.;
RT   "Identification and analysis of genes from Streptomyces pristinaespiralis
RT   encoding enzymes involved in the biosynthesis of the 4-dimethylamino-L-
RT   phenylalanine precursor of pristinamycin I.";
RL   Mol. Microbiol. 23:191-202(1997).
CC   -!- FUNCTION: Involved in pristinamycin I biosynthesis (PubMed:9044253).
CC       Catalyzes the SAM-dependent methylation of 4-amino-L-phenylalanine
CC       (PAPA) to 4-methylamino-L-phenylalanine (MMPAPA), and of MMPAPA to 4-
CC       dimethylamino-L-phenylalanine (DMPAPA) (PubMed:9044253).
CC       {ECO:0000269|PubMed:9044253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-L-phenylalanine + S-adenosyl-L-methionine = 4-
CC         methylamino-L-phenylalanine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:67960, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:143072, ChEBI:CHEBI:176804;
CC         Evidence={ECO:0000269|PubMed:9044253};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67961;
CC         Evidence={ECO:0000269|PubMed:9044253};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-methylamino-L-phenylalanine + S-adenosyl-L-methionine = 4-
CC         dimethylamino-L-phenylalanine + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:67964, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:176804, ChEBI:CHEBI:176805;
CC         Evidence={ECO:0000269|PubMed:9044253};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67965;
CC         Evidence={ECO:0000269|PubMed:9044253};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.24 mM for PAPA {ECO:0000269|PubMed:9044253};
CC         KM=0.53 mM for MMPAPA {ECO:0000269|PubMed:9044253};
CC         KM=0.10 mM for S-adenosyl-L-methionine (in the presence of PAPA)
CC         {ECO:0000269|PubMed:9044253};
CC         KM=0.12 mM for S-adenosyl-L-methionine (in the presence of MMPAPA)
CC         {ECO:0000269|PubMed:9044253};
CC         Vmax=55000 nmol/h/mg enzyme with PAPA as substrate
CC         {ECO:0000269|PubMed:9044253};
CC         Vmax=71000 nmol/h/mg enzyme with MMPAPA as substrate
CC         {ECO:0000269|PubMed:9044253};
CC         Vmax=52000 nmol/h/mg enzyme with S-adenosyl-L-methionine as substrate
CC         (in the presence of PAPA) {ECO:0000269|PubMed:9044253};
CC         Vmax=72000 nmol/h/mg enzyme with S-adenosyl-L-methionine as substrate
CC         (in the presence of MMPAPA) {ECO:0000269|PubMed:9044253};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:9044253}.
CC   -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC       family. {ECO:0000305}.
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DR   EMBL; U60417; AAC44869.1; -; Genomic_DNA.
DR   SMR; P72542; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR004556; HemK-like.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR040758; PrmC_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   Pfam; PF17827; PrmC_N; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00536; hemK_fam; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..292
FT                   /note="4-amino-L-phenylalanine/4-methylamino-L-
FT                   phenylalanine methyltransferase"
FT                   /id="PRO_0000453963"
FT   BINDING         128..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0ACC1"
SQ   SEQUENCE   292 AA;  30850 MW;  7B55A8B8E19F29FC CRC64;
     MTAAAPTLAQ ALDEATGQLT GAGITADAAR ADTRLLAAHA CQVAPGDLDT CLAGPVPPRF
     WHYVRRRLTR EPAERIVGHA YFMGHRFDLA PGVFVPKPET EEITRDAIAR LEALVRRGTT
     APLVVDLCAG PGTMAVTLAR HVPAARVLGI ELSQAAARAA RRNARGTGAR IVQGDARDAF
     PELSGTVDLV VTNPPYIPIG LRTSAPEVLE HDPPLALWAG EEGLGMIRAM ERTAARLLAP
     GGVLLLEHGS YQLASVPALF RATGRWSHAS SRPTCNDGCL TAVRNHTCAP PA