SYRB1_PSESY
ID SYRB1_PSESY Reviewed; 614 AA.
AC Q52400;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Syringomycin synthase SyrB1 {ECO:0000305};
DE EC=6.2.1.70 {ECO:0000269|PubMed:16002467, ECO:0000305|PubMed:9830033};
DE AltName: Full=L-threonine--[L-threonyl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=Syringomycin biosynthesis enzyme 1 {ECO:0000312|EMBL:AAA85160.2};
GN Name=syrB1 {ECO:0000303|PubMed:9830033};
OS Pseudomonas syringae pv. syringae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B301D;
RX PubMed=7608074; DOI=10.1128/jb.177.14.4009-4020.1995;
RA Zhang J.H., Quigley N.B., Gross D.C.;
RT "Analysis of the syrB and syrC genes of Pseudomonas syringae pv. syringae
RT indicates that syringomycin is synthesized by a thiotemplate mechanism.";
RL J. Bacteriol. 177:4009-4020(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=B301D;
RX PubMed=9830033; DOI=10.1074/jbc.273.49.32857;
RA Guenzi E., Galli G., Grgurina I., Gross D.C., Grandi G.;
RT "Characterization of the syringomycin synthetase gene cluster. A link
RT between prokaryotic and eukaryotic peptide synthetases.";
RL J. Biol. Chem. 273:32857-32863(1998).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=B301D;
RX PubMed=11277431; DOI=10.1094/mpmi.2001.14.3.336;
RA Scholz-Schroeder B.K., Hutchison M.L., Grgurina I., Gross D.C.;
RT "The contribution of syringopeptin and syringomycin to virulence of
RT Pseudomonas syringae pv. syringae strain B301D on the basis of sypA and
RT syrB1 biosynthesis mutant analysis.";
RL Mol. Plant Microbe Interact. 14:336-348(2001).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=B301D;
RX PubMed=16002467; DOI=10.1073/pnas.0504412102;
RA Vaillancourt F.H., Yin J., Walsh C.T.;
RT "SyrB2 in syringomycin E biosynthesis is a nonheme FeII alpha-
RT ketoglutarate- and O2-dependent halogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10111-10116(2005).
CC -!- FUNCTION: Involved in the biosynthesis of syringomycin E, a cyclic
CC lipodepsinonapeptide toxin with phytotoxic activity (PubMed:9830033).
CC Specifically adenylates L-threonine and loads it onto its peptidyl
CC carrier domain, via a thioester linkage to the phosphopanthetheine
CC moiety (PubMed:9830033, PubMed:16002467). Is highly specific for L-
CC threonine (PubMed:16002467). {ECO:0000269|PubMed:16002467,
CC ECO:0000269|PubMed:9830033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[peptidyl-carrier protein] + L-threonine = AMP +
CC diphosphate + L-threonyl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:61688, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15908,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144927, ChEBI:CHEBI:456215;
CC EC=6.2.1.70; Evidence={ECO:0000269|PubMed:16002467,
CC ECO:0000305|PubMed:9830033};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61689;
CC Evidence={ECO:0000269|PubMed:16002467, ECO:0000305|PubMed:9830033};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305|PubMed:16002467};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for L-threonine {ECO:0000269|PubMed:16002467};
CC KM=7.7 mM for L-serine {ECO:0000269|PubMed:16002467};
CC Note=kcat is 29.1 min(-1) with L-threonine as substrate. kcat is 1.23
CC min(-1) with L-serine as substrate. {ECO:0000269|PubMed:16002467};
CC -!- DISRUPTION PHENOTYPE: Mutant is defective in syringomycin production
CC but produces wild-type levels of syringopeptin. Mutation significantly
CC reduces the virulence of strain B301D in immature sweet cherry fruits.
CC {ECO:0000269|PubMed:11277431}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; U25130; AAA85160.2; -; Genomic_DNA.
DR RefSeq; WP_032655800.1; NZ_VBUL01000016.1.
DR KEGG; ag:AAA85160; -.
DR BioCyc; MetaCyc:MON-20501; -.
DR BRENDA; 6.2.1.70; 12469.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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 TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..614
FT /note="Syringomycin synthase SyrB1"
FT /id="PRO_0000454786"
FT DOMAIN 535..610
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 570
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 614 AA; 66144 MW; 22E77CD3A7B63388 CRC64;
MPITNTDESL SAASAPLKPG AFLHEIFSDR ARQFPERTAV SDAARTLSYA QLDALSTKLA
ARLRDEGVTY GTRVGMYLPR SVDLVTSLLG ILKAGGTYVP VDPQYPGKRV EHIVRDSELS
LIIGDAANLP KISSLRVLAL DELLSAPALQ PAAQDTRIDP NNSTAYIIYT SGSTGEPKGV
QVSHGNVSRL LESTQRAYGF NAQDVWSMFH SIGFDFSVWE IWGALAHGGQ VAVVPYDISR
SPAALRQWLA DQRITVLSQT PSAFRGLDEA DRGNTAPLAL RYVVLGGEAL PASVLRPWVE
RHGDQKPALI NMYGITEATV HTTFKRVLAQ DLETAAMVSL GKPLDGWRLH LLDANQAPVA
AGTTGELYIE GAGVAQGYLN REALNVERFV ELPGAVRAYR TGDLMTLESN GEYRYAGRCD
EQLKISGFRI EPGEIEASLQ TSPSVAAAHV GVHDYGDGDL RLVAYVVPGQ GVDAWTEQAR
SEVAALMAEN LPGYMRPSVY VPLAELPVTH HGKIDKQQLP SPAAGTALSG AADVKGLSEQ
EHFVLKVWSE DLGLKNIGVN DDFFDSGGTS LALIRSLSKL KTHYKINLDP GILADGATAK
VLADHITRSL VQAH
