PMSD_PSEE4
ID PMSD_PSEE4 Reviewed; 1438 AA.
AC Q1IAL0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Pseudomonine synthase PmsD {ECO:0000305};
DE EC=6.2.1.70 {ECO:0000269|PubMed:18710233};
DE AltName: Full=L-threonine--[L-threonyl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=Nonribosomal peptide synthase PmsD {ECO:0000305};
GN Name=pmsD {ECO:0000303|PubMed:18710233};
GN Synonyms=basA {ECO:0000312|EMBL:CAK15307.1};
GN OrderedLocusNames=PSEEN2503 {ECO:0000312|EMBL:CAK15307.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48;
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=L48;
RX PubMed=18710233; DOI=10.1021/ja804499r;
RA Sattely E.S., Walsh C.T.;
RT "A latent oxazoline electrophile for N-O-C bond formation in pseudomonine
RT biosynthesis.";
RL J. Am. Chem. Soc. 130:12282-12284(2008).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore pseudomonine.
CC Specifically adenylates L-threonine and loads it onto a peptidyl
CC carrier protein, via a thioester linkage to the phosphopanthetheine
CC moiety (PubMed:18710233). May function in trans to generate substrate-
CC bound PmsG (PubMed:18710233). Activates proteinogenic L-Thr
CC preferentially over L-allo-Thr or D-Thr (PubMed:18710233).
CC {ECO:0000269|PubMed:18710233}.
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:18710233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61689;
CC Evidence={ECO:0000269|PubMed:18710233};
CC -!- PATHWAY: Siderophore biosynthesis; pseudomonine biosynthesis.
CC {ECO:0000269|PubMed:18710233}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CT573326; CAK15307.1; -; Genomic_DNA.
DR RefSeq; WP_011533706.1; NC_008027.1.
DR STRING; 384676.PSEEN2503; -.
DR EnsemblBacteria; CAK15307; CAK15307; PSEEN2503.
DR KEGG; pen:PSEEN2503; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_1_6; -.
DR OMA; MNTVEFI; -.
DR OrthoDB; 572620at2; -.
DR BioCyc; MetaCyc:MON-20464; -.
DR UniPathway; UPA00024; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Ligase.
FT CHAIN 1..1438
FT /note="Pseudomonine synthase PmsD"
FT /id="PRO_0000454821"
SQ SEQUENCE 1438 AA; 157161 MW; 1C720E81FFDAB59A CRC64;
MRELTSMQAA CWIGRTAHAA LGKVSAHLYA EFDGHAIDLE RLRAALQQVS LLHPMLRLRI
DQDGLQGIAP MEQAPRLEVD DLRGLAEPEV AQRLLRKREA WTHQQLDLRH GCAARFSVSQ
LEGERSRLHV DTDMIAIDPS SLRVLMEDLA RCYEAPDAPV ATPPSFFAWW DAVRADPALK
ATQERDRQWW RARLDSIAPA PTLPLLDVQP AQAHSQRLTT WLDANQHIAL RQLARERKVT
LSTLMLGLFA SALGAQTGDR QFRLNVPSFW RAPLIDGVER IVGEFANVLI VDVDLDAAPD
IAALCNQLAK TTAACMAHSA YPGVNLMRDL SRHHGTPQLA PVVFTAALDM PGKELFSPRV
KNAFGPLGWL ISQGPQVALD AQIACADGGI LINWDIRLDA LPEAWVTQLF ERFVDLASEV
ARQPATLDQA LPRAPEKRPL NPLQQAYLLG RTTQMPLGGV AMQEFREYRG MMDSAVLRSR
LDAMVRRHPS LRTRIDADRR VQYVSDEVRL NLDEVDLGHL PLAEALGVID ARREDYAHAL
SPLDRSPWNV TVFHLAHGER VVFVRLDALI LDGRSIATLL VELFEGQLEE TPQVDTGAPK
ADQTEQRTAD AAYWNTKLAA VDGAPRLPWS VPLDQAGVAR YERQSLVVPR ETFKKFCMVG
ARQRLFKNTT LMAVILEVLS HWVSEGGLCV AVPVAPPSDA AFANRSSFLA INWNRAAGSF
AERSAGLQVD VLEGLQHLAY SGVDLARQLF ERHGPGPVLP VVITNGFSWP VAPSDSAMRL
QGGLTQTPQV AMDIRFWADA DGALQLDIDY AREVLAPALV SDFLGTLGRA IGQIAGAGEF
ALAPAALIDT DHYRLNSPVE AACRDGYLAR IADHLFTPGN HKTALISGER RLSYSELGDG
VARIIAALRA RGIGQGQVVA ICLPRSPEHT MLTLACALTG VIWVPIDVAA PAERRHYLLE
NCHPDLVVLG QAQTLEQPST TCAALLATPA AAPGHLADLS LNEAPGYYLY TSGTTGKPKC
VVLNNRATAN VIGSTLAEWR VTERDVFLSV TPLHHDMSVF DVFGSLAAGA TLVLPAPGED
KDALRWNQLV AEHQVTLWCS VPAILEMLLA CRGEHGLQSL RLIAQGGDYI KPAVIAGLRE
LLPQARLISL GGPTETTIWS IWHEIGADDR KLIPYGRPLP GNRYFVLDAQ GRHCPVGVVG
RIHTAGANLA LGYLLDGALQ QSDFITVDDE HGQAVRAFRT GDCGRYRVDG TLLFDSRVNG
YVKVRGVRVS LPDIEMVLNQ HPALRHVLVV DYGEPRLGEV CLGALYVCDP QAAEPSMAEL
RDYAREHLPH SHVPTRLLGV AALPLSQNGK PDRRRARELL SAPATASVRD KVLAIYLQVL
GHSNEAGTDS AVDFISLGLR PPHLKAVAAQ LQAQFGVSLS PGQLLRCRNA QEVERLLG
