PIGA_SERS3
ID PIGA_SERS3 Reviewed; 386 AA.
AC Q5W271;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=L-prolyl-[peptidyl-carrier protein] dehydrogenase {ECO:0000305};
DE EC=1.3.8.14 {ECO:0000305|PubMed:15853884};
DE AltName: Full=Flavoprotein desaturase PigA {ECO:0000303|PubMed:17002325};
DE AltName: Full=L-prolyl-PCP dehydrogenase {ECO:0000303|PubMed:15853884};
GN Name=pigA {ECO:0000303|PubMed:15528645};
OS Serratia sp. (strain ATCC 39006).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia; unclassified Serratia.
OX NCBI_TaxID=104623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=15528645; DOI=10.1099/mic.0.27222-0;
RA Harris A.K., Williamson N.R., Slater H., Cox A., Abbasi S., Foulds I.,
RA Simonsen H.T., Leeper F.J., Salmond G.P.;
RT "The Serratia gene cluster encoding biosynthesis of the red antibiotic,
RT prodigiosin, shows species- and strain-dependent genome context
RT variation.";
RL Microbiology 150:3547-3560(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, COFACTOR, AND PATHWAY.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=15853884; DOI=10.1111/j.1365-2958.2005.04602.x;
RA Williamson N.R., Simonsen H.T., Ahmed R.A., Goldet G., Slater H.,
RA Woodley L., Leeper F.J., Salmond G.P.;
RT "Biosynthesis of the red antibiotic, prodigiosin, in Serratia:
RT identification of a novel 2-methyl-3-n-amyl-pyrrole (MAP) assembly pathway,
RT definition of the terminal condensing enzyme, and implications for
RT undecylprodigiosin biosynthesis in Streptomyces.";
RL Mol. Microbiol. 56:971-989(2005).
RN [3]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 39006 / SC 11482;
RX PubMed=17002325; DOI=10.1021/ja063611l;
RA Garneau-Tsodikova S., Dorrestein P.C., Kelleher N.L., Walsh C.T.;
RT "Protein assembly line components in prodigiosin biosynthesis:
RT characterization of PigA,G,H,I,J.";
RL J. Am. Chem. Soc. 128:12600-12601(2006).
CC -!- FUNCTION: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-
CC carbaldehyde (MBC), one of the terminal products involved in the
CC biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the
CC desaturation of the L-prolyl-[PigG] to yield 1H-pyrrole-2-carbonyl-
CC [PigG]. {ECO:0000269|PubMed:15853884, ECO:0000269|PubMed:17002325}.
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:0000305|PubMed:15853884};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P26440, ECO:0000305|PubMed:15853884};
CC -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC {ECO:0000305|PubMed:15853884, ECO:0000305|PubMed:17002325}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a white phenotype.
CC {ECO:0000269|PubMed:15853884}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ833001; CAH55629.1; -; Genomic_DNA.
DR RefSeq; WP_021014639.1; NZ_CP025085.1.
DR PDB; 5ZW0; X-ray; 2.54 A; A/B=1-386.
DR PDB; 5ZW2; X-ray; 1.80 A; A=1-386.
DR PDB; 5ZW7; X-ray; 1.30 A; A=1-386.
DR PDB; 5ZW8; X-ray; 1.69 A; A=1-386.
DR PDB; 6AF6; X-ray; 1.62 A; A=1-386.
DR PDBsum; 5ZW0; -.
DR PDBsum; 5ZW2; -.
DR PDBsum; 5ZW7; -.
DR PDBsum; 5ZW8; -.
DR PDBsum; 6AF6; -.
DR AlphaFoldDB; Q5W271; -.
DR SMR; Q5W271; -.
DR STRING; 104623.Ser39006_01369; -.
DR KEGG; ag:CAH55629; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 760677at2; -.
DR BRENDA; 1.3.8.14; 5690.
DR UniPathway; UPA01072; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
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 3D-structure; Antibiotic biosynthesis; FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..386
FT /note="L-prolyl-[peptidyl-carrier protein] dehydrogenase"
FT /id="PRO_0000436158"
FT ACT_SITE 244
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 125..134
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 158..160
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 270
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 338..342
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 367..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT HELIX 7..22
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:5ZW7"
FT TURN 49..54
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 83..95
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5ZW7"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:5ZW7"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 250..269
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 281..309
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 315..340
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:5ZW7"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:5ZW7"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:5ZW7"
FT HELIX 368..378
FT /evidence="ECO:0007829|PDB:5ZW7"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:5ZW7"
SQ SEQUENCE 386 AA; 42048 MW; 2AC23337D65A801C CRC64;
MDFNLSNSQS DIYESAYRFA CDVLDQDAQT RISQKILSTE LWKKAAAYGF AHGPVSHQFG
GSELGALDTA LMIEALGKGS RDIGLSFSLC AHLCACVIPL YRFGSSELKD KYLESLVTGK
LIAANAATEP DAGSDIYNMQ ATAQPCEGGY ILNGKKIFIT NAPIADVFII YAKTNPDHGF
LGVSAFLIEK GTPGLNVGEV IPKDCLSNCP WSEIVFNDIF IPQSQRIGME GAGGAIFHDS
MIWEKGCLSA LFVGGLARLL ETTLEYAKAR QQFGKAIGQF QSVSNRIIDM KLRLEQCRLM
LYRACWKHDQ GQDAEADIAM SKLLISEYAV QSGLDAIQTF GGAAMDQELG LVRHLLNMIP
SRIFSGTNDI QKEIIARKLG LRGTSS
