CMAA_PSESG
ID CMAA_PSESG Reviewed; 595 AA.
AC Q6TNA5;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase {ECO:0000305};
DE EC=6.2.1.46 {ECO:0000269|PubMed:14679222};
DE AltName: Full=Adenylation activation enzyme {ECO:0000303|PubMed:14679222};
DE AltName: Full=Coronamic acid synthetase CmaA {ECO:0000303|PubMed:14679222};
GN Name=CmaA {ECO:0000303|PubMed:14679222}; ORFNames=ALO37_100711;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP SUBUNIT.
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.
CC -!- FUNCTION: Involved in the biosynthesis of the phytotoxin coronatine
CC (COR) which mimics the plant hormone jasmonic acid isoleucine and
CC promotes opening of stomata for bacterial entry, bacterial growth in
CC the apoplast, systemic susceptibility, and disease symptoms. CmaA
CC catalyzes the adenylation of L-allo-isoleucine (via the A domain) and
CC the attachment of L-allo-isoleucine to the 4'-phosphopantetheine arm
CC located within the T domain of CmaA. It can also use L-isoleucine, L-
CC leucine and L-valine as substrates. {ECO:0000269|PubMed:14679222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[CmaA peptidyl-carrier protein] + L-alloisoleucine
CC = AMP + diphosphate + L-alloisoleucyl-[CmaA peptidyl-carrier
CC protein]; Xref=Rhea:RHEA:45624, Rhea:RHEA-COMP:11295, Rhea:RHEA-
CC COMP:11297, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:85338, ChEBI:CHEBI:85339, ChEBI:CHEBI:456215;
CC EC=6.2.1.46; Evidence={ECO:0000269|PubMed:14679222};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305|PubMed:14679222};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000305|PubMed:14679222};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for L-allo-isoleucine (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC KM=0.84 mM for D-allo-isoleucine (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC KM=1 mM for L-isoleucine (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC KM=1.1 mM for D-isoleucine (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC KM=1.5 mM for DL-coronamic acid (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC KM=7.4 mM for L-leucine (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC KM=8.2 mM for L-valine (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC KM=11 mM for DL-norcoronamic acid (at pH 7.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:14679222};
CC Note=kcat is 17 min(-1) for ligase activity with L-allo-isoleucine as
CC substrate (at pH 7.5 and 25 degrees Celsius). kcat is 16 min(-1) for
CC ligase activity with L-leucine as substrate (at pH 7.5 and 25 degrees
CC Celsius). kcat is 12 min(-1) for ligase activity with L-valine as
CC substrate (at pH 7.5 and 25 degrees Celsius). kcat is 6.7 min(-1) for
CC ligase activity with DL-coronamic acid as substrate (at pH 7.5 and 25
CC degrees Celsius). kcat is 2.8 min(-1) for ligase activity with L-
CC isoleucine as substrate (at pH 7.5 and 25 degrees Celsius). kcat is
CC 1.1 min(-1) for ligase activity with D-isoleucine and DL-norcoronamic
CC acid as substrates (at pH 7.5 and 25 degrees Celsius). kcat is 0.2
CC min(-1) for ligase activity with D-allo-isoleucine as substrate (at
CC pH 7.5 and 25 degrees Celsius). {ECO:0000269|PubMed:14679222};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14679222}.
CC -!- DOMAIN: The didomain protein contains an adenylation domain (A domain)
CC and a thiolation domain (T domain). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY391839; AAQ93484.1; -; Genomic_DNA.
DR EMBL; LJQL01000191; KPX44542.1; -; Genomic_DNA.
DR RefSeq; WP_004666822.1; NZ_RBVH01000262.1.
DR AlphaFoldDB; Q6TNA5; -.
DR SMR; Q6TNA5; -.
DR EnsemblBacteria; KPX44542; KPX44542; ALO37_100711.
DR KEGG; ag:AAQ93484; -.
DR PATRIC; fig|318.3.peg.2001; -.
DR Proteomes; UP000050447; Unassembled WGS sequence.
DR GO; GO:0016878; F:acid-thiol ligase activity; IDA:UniProtKB.
DR GO; GO:0010188; P:response to microbial phytotoxin; IDA:UniProtKB.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Plasmid; Virulence.
FT CHAIN 1..595
FT /note="L-allo-isoleucine:holo-[CmaA peptidyl-carrier
FT protein] ligase"
FT /id="PRO_0000435661"
FT DOMAIN 507..582
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 542
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 595 AA; 65930 MW; 1F1CD9490D5FAAF6 CRC64;
MTSYHSHPPK AYRRFESVCT QAPNAIAVVH EGKPVTYQQL QTQVLERSEA LIRQGLADHP
YMPLMANRCL EYLITMLACC KLGITYVSIE PSTPSKRLIA VLEQLGCNHL LLLGQPTDLR
PDPTLTCFRL DDCGTLCSDG PALRQPIRRR LDDASVITVM FTSGTTGVPK GVRISQDGLL
NLVDNVQQQV QGKPRSYVHH SSIGFDAALF EVWVPLLTGA CVTLQPSEFN IDALDHCVRA
ASCDVLLLTT SLFHLVAQHR LSMLEAVRVL YVGGEVLKPV HARALLLANP RITLVNGYGP
TENTVFSTWY SLNKPEDAER DVIPIGQFLH QVHGKIVDAK LQEVEVGTPG ELLLTGANLA
LGYLDEALTP TRFLQLPEGT YYRTGDYVIQ DEHGMLFYQG RIDEQVKIKG FRVEIAEVEH
ALTQLPGVAQ AVVQAHVMND LENSLHAFIV FRHGSPTIEE SKLMSLLGDR LPHYMVPRRI
HYLAELPLTA NGKVDKRSLQ PPEKAAVVSP QAGSAVLEIW SGILGTRNLQ LEHSIYGYGA
SSLSVVMAHS RINEILGRTT PFDEVARLST FQEWVQYYAT HADPVTSLRS QHGNH
