CMAE_PSESG
ID CMAE_PSESG Reviewed; 282 AA.
AC Q6TNA6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=L-allo-isoleucyltransferase {ECO:0000305};
DE EC=2.3.2.28 {ECO:0000269|PubMed:16121186, ECO:0000269|PubMed:17530782};
DE AltName: Full=Aminoacyltransferase CmaE {ECO:0000303|PubMed:17530782};
GN Name=cmaE {ECO:0000303|PubMed:14679222};
GN ORFNames=ALO37_00083 {ECO:0000312|EMBL:KPX44543.1},
GN ALP27_100733 {ECO:0000312|EMBL:RMU44151.1},
GN ALQ13_00274 {ECO:0000312|EMBL:RMP96815.1},
GN ALQ75_02075 {ECO:0000312|EMBL:RMM81474.1};
OS Pseudomonas savastanoi pv. glycinea (Pseudomonas syringae pv. glycinea).
OG Plasmid p4180A.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=318;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PG4180; PLASMID=p4180A;
RX PubMed=14679222; DOI=10.1128/jb.186.1.35-42.2004;
RA Couch R., O'Connor S.E., Seidle H., Walsh C.T., Parry R.;
RT "Characterization of CmaA, an adenylation-thiolation didomain enzyme
RT involved in the biosynthesis of coronatine.";
RL J. Bacteriol. 186:35-42(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP2189;
RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT "Genome announcement of multiple Pseudomonas syringae strains.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 4402, ICMP 5027, and ICMP 5560;
RA Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.;
RT "Recombination of ecologically and evolutionarily significant loci
RT maintains genetic cohesion in the Pseudomonas syringae species complex.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-105.
RX PubMed=16121186; DOI=10.1038/nature03797;
RA Vaillancourt F.H., Yeh E., Vosburg D.A., O'Connor S.E., Walsh C.T.;
RT "Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino
RT acid biosynthesis.";
RL Nature 436:1191-1194(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-105.
RX PubMed=17530782; DOI=10.1021/bi700243h;
RA Strieter E.R., Vaillancourt F.H., Walsh C.T.;
RT "CmaE: a transferase shuttling aminoacyl groups between carrier protein
RT domains in the coronamic acid biosynthetic pathway.";
RL Biochemistry 46:7549-7557(2007).
CC -!- FUNCTION: Involved in the biosynthesis of the phytotoxin coronatine
CC (COR). Catalyzes the transfer of the aminoacyl group covalently
CC attached to the pantetheinyl arm of CmaA to the holo-pantetheinyl arm
CC of CmaD. During the shuttling process, CmaE generates a covalent-
CC aminoacyl-S-Cys enzyme intermediate by the action of its donor
CC substrate L-aminoacyl-S-CmaA and delivers it to the sulfhydryl group
CC attached to the phosphopantetheinyl arm on CmaD.
CC {ECO:0000269|PubMed:16121186, ECO:0000269|PubMed:17530782}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[CmaD peptidyl-carrier protein] + L-alloisoleucyl-[CmaA
CC peptidyl-carrier protein] = holo-[CmaA peptidyl-carrier protein] + L-
CC alloisoleucyl-[CmaD peptidyl-carrier protein]; Xref=Rhea:RHEA:45628,
CC Rhea:RHEA-COMP:11295, Rhea:RHEA-COMP:11297, Rhea:RHEA-COMP:11299,
CC Rhea:RHEA-COMP:11300, ChEBI:CHEBI:64479, ChEBI:CHEBI:85339;
CC EC=2.3.2.28; Evidence={ECO:0000269|PubMed:16121186,
CC ECO:0000269|PubMed:17530782};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45629;
CC Evidence={ECO:0000269|PubMed:16121186, ECO:0000269|PubMed:17530782};
CC -!- MISCELLANEOUS: In vitro, is able to accept L-Phe as a substrate when
CC presented on CmaD and is able to load this aminoacyl moiety onto
CC heterologous T domains. Thus, CmaE should be useful for shuttling
CC different aminoacyl groups between T domains existing within
CC heterologous nonribosomal peptide-synthetase (NRPS) assembly lines to
CC generate natural product-like derivatives.
CC {ECO:0000269|PubMed:17530782}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AY391839; AAQ93483.1; -; Genomic_DNA.
DR EMBL; LJQL01000191; KPX44543.1; -; Genomic_DNA.
DR EMBL; RBOL01000131; RMM81474.1; -; Genomic_DNA.
DR EMBL; RBQV01000254; RMP96815.1; -; Genomic_DNA.
DR EMBL; RBUC01000704; RMU44151.1; -; Genomic_DNA.
DR RefSeq; WP_004666821.1; NZ_RBVH01000262.1.
DR AlphaFoldDB; Q6TNA6; -.
DR ESTHER; psesy-PSPTO4708; 6_AlphaBeta_hydrolase.
DR EnsemblBacteria; KPX44543; KPX44543; ALO37_00083.
DR EnsemblBacteria; RMM81474; RMM81474; ALQ75_02075.
DR EnsemblBacteria; RMP96815; RMP96815; ALQ13_00274.
DR EnsemblBacteria; RMU44151; RMU44151; ALP27_100733.
DR PATRIC; fig|318.3.peg.2000; -.
DR Proteomes; UP000050447; Unassembled WGS sequence.
DR Proteomes; UP000276166; Unassembled WGS sequence.
DR Proteomes; UP000282052; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Plasmid; Transferase.
FT CHAIN 1..282
FT /note="L-allo-isoleucyltransferase"
FT /id="PRO_0000452006"
FT DOMAIN 169..261
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 105
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:16121186,
FT ECO:0000305|PubMed:17530782"
FT MUTAGEN 105
FT /note="C->A: Abolishes transferase activity."
FT /evidence="ECO:0000269|PubMed:16121186,
FT ECO:0000269|PubMed:17530782"
SQ SEQUENCE 282 AA; 31809 MW; F185A4B70B35D35F CRC64;
MHSLFTLNLD LERAGKVICA QSLPFDTARE TLLLLSPVGT QCCYMKNAAL FLISHFNLII
LESDTWLAYA NEAGVNPEEG VADFIRQFNA ALPEPVRVDA LVGYCSSAPL ALLAANQGAC
RTLLLLNGAY FLKDDGVIKS QYERDVERMM QSIPQGNCAQ VYEAVSLLHT QSTYTPSDYR
YQQVRPLREL SAFRQYLTFL NNLASLELVR IAQAVKTPTL VWCGSQDRYT DTASSRYIAQ
LLPHSELVED PDGQHHDFVD GHERLYLTMT RFLTRHKQRA IQ
