AMTA_PSESH
ID AMTA_PSESH Reviewed; 362 AA.
AC Q9RBU1;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=L-arginine:L-lysine amidinotransferase {ECO:0000303|PubMed:11310742};
DE EC=2.1.4.3 {ECO:0000269|PubMed:11310742, ECO:0000269|PubMed:27419063};
GN Name=amtA {ECO:0000303|PubMed:11310742};
GN Synonyms=txi12 {ECO:0000312|EMBL:BAF32885.1};
OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS phaseolicola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=NPS 3121;
RX PubMed=11310742; DOI=10.1094/mpmi.2001.14.4.545;
RA Hernandez-Guzman G., Alvarez-Morales A.;
RT "Isolation and characterization of the gene coding for the
RT amidinotransferase involved in the biosynthesis of phaseolotoxin in
RT Pseudomonas syringae pv. phaseolicola.";
RL Mol. Plant Microbe Interact. 14:545-554(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MAFF 302282;
RX PubMed=16927007; DOI=10.1007/s00239-005-0271-4;
RA Genka H., Baba T., Tsuda M., Kanaya S., Mori H., Yoshida T., Noguchi M.T.,
RA Tsuchiya K., Sawada H.;
RT "Comparative analysis of argK-tox clusters and their flanking regions in
RT phaseolotoxin-producing Pseudomonas syringae pathovars.";
RL J. Mol. Evol. 63:401-414(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=NPS 3121;
RX PubMed=17237165; DOI=10.1128/jb.01845-06;
RA Aguilera S., Lopez-Lopez K., Nieto Y., Garciduenas-Pina R.,
RA Hernandez-Guzman G., Hernandez-Flores J.L., Murillo J., Alvarez-Morales A.;
RT "Functional characterization of the gene cluster from Pseudomonas syringae
RT pv. phaseolicola NPS3121 involved in synthesis of phaseolotoxin.";
RL J. Bacteriol. 189:2834-2843(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF MET-240; HIS-241 AND
RP MET-243.
RC STRAIN=1448A;
RX PubMed=27419063; DOI=10.1002/2211-5463.12071;
RA Li M., Chen L., Deng Z., Zhao C.;
RT "Characterization of AmtA, an amidinotransferase involved in the
RT biosynthesis of phaseolotoxins.";
RL FEBS Open Bio 6:603-609(2016).
CC -!- FUNCTION: Involved in the biosynthesis of phaseolotoxin, a nonhost-
CC specific toxin which is a key component in the development of the halo
CC blight disease of beans (PubMed:11310742). Catalyzes the transfer of an
CC amidino group from arginine to lysine to produce one molecule of
CC homoarginine and one molecule of ornithine, both being precursors in
CC the biosynthesis of phaseolotoxin (PubMed:11310742, PubMed:27419063).
CC Can also use L-canavanine as an alternative amidine donor with L-
CC ornithine as amidine acceptor (PubMed:27419063).
CC {ECO:0000269|PubMed:11310742, ECO:0000269|PubMed:27419063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine + L-lysine = L-homoarginine + L-ornithine;
CC Xref=Rhea:RHEA:59240, ChEBI:CHEBI:32551, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:143006; EC=2.1.4.3;
CC Evidence={ECO:0000269|PubMed:11310742, ECO:0000269|PubMed:27419063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-canavanine + L-ornithine = H(+) + L-arginine + L-canaline;
CC Xref=Rhea:RHEA:62444, ChEBI:CHEBI:15378, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:78902, ChEBI:CHEBI:145769; EC=2.1.4.3;
CC Evidence={ECO:0000269|PubMed:27419063};
CC -!- DISRUPTION PHENOTYPE: Mutant loses the ability to synthesize
CC homoarginine and phaseolotoxin under permissive conditions.
CC {ECO:0000269|PubMed:11310742, ECO:0000269|PubMed:17237165}.
CC -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000305}.
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DR EMBL; AF186235; AAD56249.1; -; Genomic_DNA.
DR EMBL; AB237164; BAF32885.1; -; Genomic_DNA.
DR EMBL; DQ141263; AAZ99811.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RBU1; -.
DR SMR; Q9RBU1; -.
DR GO; GO:0015067; F:amidinotransferase activity; IEA:InterPro.
DR InterPro; IPR033195; AmidinoTrfase.
DR PANTHER; PTHR10488; PTHR10488; 1.
PE 1: Evidence at protein level;
KW Transferase.
FT CHAIN 1..362
FT /note="L-arginine:L-lysine amidinotransferase"
FT /id="PRO_0000450559"
FT ACT_SITE 195
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT ACT_SITE 244
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT ACT_SITE 346
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT MUTAGEN 240
FT /note="M->P: No change in activity and substrate
FT specificity."
FT /evidence="ECO:0000269|PubMed:27419063"
FT MUTAGEN 241
FT /note="H->N: No change in activity and substrate
FT specificity."
FT /evidence="ECO:0000269|PubMed:27419063"
FT MUTAGEN 243
FT /note="M->S: Abolishes amidinotransferase activity."
FT /evidence="ECO:0000269|PubMed:27419063"
SQ SEQUENCE 362 AA; 41362 MW; 8FC8AE7430F1B2C2 CRC64;
MKKIQTFIQT SPVCSYTEWD LLEEIIVGVV DGACIPPWHA AMEPCLPTQQ HQFFRDNAGK
PFPQERIDLA RKELDEFARI LECEGVKVRR PEPKNQSLVY GAPGWSSTGM YAAMPRDVLL
VVGTDIIECP LAWRSRYFET AAYKKLLKEY FHGGAKWSSG PKPELSDEQY VDGWVEDEAA
TSANLVITEF EPTFDAADFT RLGKDIIAQK SNVTNEFGIN WLQRHLGDDY KIHVLEFNDM
HPMHIDATLV PLAPGKLLIN PERVQKMPEI FRGWDAIHAP KPIMPDSHPL YMTSKWINMN
ILMLDERRVV VERQDEPMIK AMKGAGFEPI LCDFRNFNSF GGSFHCATVD IRRRGKLESY
LV
