REDW_STRCO
ID REDW_STRCO Reviewed; 391 AA.
AC O54143;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=L-prolyl-[peptidyl-carrier protein] dehydrogenase {ECO:0000305};
DE EC=1.3.8.14 {ECO:0000269|PubMed:11880032};
GN Name=redW {ECO:0000303|PubMed:11514230};
GN OrderedLocusNames=SCO5879 {ECO:0000312|EMBL:CAA16488.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP GENE CLUSTER, AND FUNCTION.
RX PubMed=11514230; DOI=10.1016/s1074-5521(01)00054-0;
RA Cerdeno A.M., Bibb M.J., Challis G.L.;
RT "Analysis of the prodiginine biosynthesis gene cluster of Streptomyces
RT coelicolor A3(2): new mechanisms for chain initiation and termination in
RT modular multienzymes.";
RL Chem. Biol. 8:817-829(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
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 undecylprodigiosin
CC (PubMed:11514230, PubMed:11880032). Catalyzes the desaturation of the
CC L-prolyl-[prolyl-carrier protein] to yield 1H-pyrrole-2-carbonyl-
CC [prolyl-carrier protein] (PubMed:11880032).
CC {ECO:0000269|PubMed:11514230, 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:0000269|PubMed:11880032};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL939125; CAA16488.1; -; Genomic_DNA.
DR PIR; T34831; T34831.
DR RefSeq; NP_630001.1; NC_003888.3.
DR RefSeq; WP_003973142.1; NZ_VNID01000007.1.
DR AlphaFoldDB; O54143; -.
DR SMR; O54143; -.
DR STRING; 100226.SCO5879; -.
DR GeneID; 1101321; -.
DR KEGG; sco:SCO5879; -.
DR PATRIC; fig|100226.15.peg.5978; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_11; -.
DR InParanoid; O54143; -.
DR OMA; YRACWLL; -.
DR PhylomeDB; O54143; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
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..391
FT /note="L-prolyl-[peptidyl-carrier protein] dehydrogenase"
FT /id="PRO_0000444034"
FT ACT_SITE 246
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
SQ SEQUENCE 391 AA; 41624 MW; 95E01740EC1EB755 CRC64;
MNFDFDAGFD TETRELRDMV VRFARRELDS SGRFDDAEDF RRRWLLAGKQ GLTGTTVPGE
YGGSGLDAVS AAATMEALGY GCADTGFAFS VAAHLFAAVM PIVEFGTGEQ RAAWLPALCS
GERIAAHAIT EPEAGSDALH LRTRARPVDD GHVLSGSKCF ITNAPVADVF VVQAATDPRG
GFFGLTTFLV EASTPGLTVG RPYDKVGLRG SPTADVHFDD CYVPAGAVLG AEGSGASIFS
SSMKWERTCL FAAYLGAMRR VLESTVDHVR DREQFGSPIG GFQAVSHRIV DMLGRYEGAR
LLLYRAARSL SDGTADEVGP ALAKIAVSEA AVQLGLDAVQ LRGGLGIMDG EAETLLRDAL
PARIFSGTNE IQKNNVARAL GLGRRRPAAR R
