ID   PLTE_PSEF5              Reviewed;         380 AA.
AC   Q4KCY6;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=L-prolyl-[peptidyl-carrier protein] dehydrogenase {ECO:0000305};
DE            EC=1.3.8.14 {ECO:0000269|PubMed:11880032};
GN   Name=pltE {ECO:0000312|EMBL:AAY92063.1};
GN   OrderedLocusNames=PFL_2791 {ECO:0000312|EMBL:AAY92063.1};
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=11880032; DOI=10.1016/s1074-5521(02)00100-x;
RA   Thomas M.G., Burkart M.D., Walsh C.T.;
RT   "Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during
RT   undecylprodigiosin and pyoluteorin biosynthesis.";
RL   Chem. Biol. 9:171-184(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of pyoluteorin. Catalyzes the
CC       desaturation of the L-prolyl-[PltL] to yield 1H-pyrrole-2-carbonyl-
CC       [PltL]. {ECO:0000269|PubMed:11880032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-prolyl-[peptidyl-carrier protein] + 2 oxidized
CC         [electron-transfer flavoprotein] = (1H-pyrrole-2-carbonyl)-[peptidyl-
CC         carrier protein] + 2 reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:55152, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         Rhea:RHEA-COMP:14109, Rhea:RHEA-COMP:14110, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:138622,
CC         ChEBI:CHEBI:138623; EC=1.3.8.14;
CC         Evidence={ECO:0000269|PubMed:11880032};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000305|PubMed:11880032};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000076; AAY92063.1; -; Genomic_DNA.
DR   RefSeq; WP_011061083.1; NC_004129.6.
DR   AlphaFoldDB; Q4KCY6; -.
DR   SMR; Q4KCY6; -.
DR   STRING; 220664.PFL_2791; -.
DR   PRIDE; Q4KCY6; -.
DR   EnsemblBacteria; AAY92063; AAY92063; PFL_2791.
DR   GeneID; 57475842; -.
DR   KEGG; pfl:PFL_2791; -.
DR   PATRIC; fig|220664.5.peg.2847; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_6; -.
DR   OMA; VHRWAQE; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; MetaCyc:MON-20314; -.
DR   Proteomes; UP000008540; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:JCVI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..380
FT                   /note="L-prolyl-[peptidyl-carrier protein] dehydrogenase"
FT                   /id="PRO_0000444033"
FT   ACT_SITE        243
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P26440"
FT   BINDING         269
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P26440"
FT   BINDING         280
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P26440"
SQ   SEQUENCE   380 AA;  41058 MW;  C6CAA4801EBC6CD6 CRC64;
     MDFNYDDTQK KHAAMIAQVC AEQLAACGNE HSRYFTARQW AICGEAGLLG LSIPREYGGQ
     GLGALSTAIA MHAFGLGCTD MGLVFAAAAH QFACAMPIVE FATAETKRDV LPKLASGEFI
     GSNAITEPEA GSDSSNLKSR AWPQADGSYR LDGHKSFAGN APIADIFVTY ATTQPEYGAL
     GVSGFIVHRS SAGLRVSEPL DKVCLRSCPA GEVFFDDCRV PEVNRLGEEG QGRQVFQSSM
     GWERACLFAA FLGMMERQLE QTIEHARTRR QFGKPIGDNQ AVSHRIAQMK LRLESARLLL
     FRACWGMDQG DPGQLNIALS KLAISEGALA SSIDAVRIFG GRGCLESFGI EAMLRDSIGT
     TIFSGTSDMQ HEIIARELKL