PIGB_SERS3
ID PIGB_SERS3 Reviewed; 670 AA.
AC Q5W270;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Oxidoreductase PigB {ECO:0000305|PubMed:15853884};
DE EC=1.-.-.-;
DE Flags: Precursor;
GN Name=pigB {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, 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).
CC -!- FUNCTION: Involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole
CC (MAP), one of the terminal products involved in the biosynthesis of the
CC red antibiotic prodigiosin (Pig). Catalyzes the oxidation of dihydro
CC form of MAP (H2MAP) to yield MAP. {ECO:0000269|PubMed:15853884}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:15853884};
CC -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC {ECO:0000305|PubMed:15853884}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a white phenotype
CC and produce 4-hydroxy-2,2'-bipyrrole-5-carbaldehyde (HBC), 4- methoxy-
CC 2,2'-bipyrrole-5-carbaldehyde (MBC) and a dihydro form of MAP (H2MAP).
CC {ECO:0000269|PubMed:15853884}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ833001; CAH55630.1; -; Genomic_DNA.
DR RefSeq; WP_021014640.1; NZ_CP025085.1.
DR AlphaFoldDB; Q5W270; -.
DR SMR; Q5W270; -.
DR STRING; 104623.Ser39006_01370; -.
DR KEGG; ag:CAH55630; -.
DR eggNOG; COG1232; Bacteria.
DR OrthoDB; 198804at2; -.
DR UniPathway; UPA01072; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IMP:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR046104; DUF6041.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF19507; DUF6041; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; FAD; Flavoprotein; Membrane; Oxidoreductase;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..670
FT /note="Oxidoreductase PigB"
FT /id="PRO_0000436236"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 670 AA; 73860 MW; FBEC987FE25C2CA1 CRC64;
MIIQRLFGIL YMLAGLAKAF PQFENVPAVL RQAAIANQGT WYAAASIWLG AHGDVINILV
GVVLFGSGVI LMLNPLWTTL VIYAQLLMMA VFVVILHQSQ PQVMLLDGVF ALAALYMLRG
QYHRKPKPRT FPTTSFSLPT PSSESSFSAP LGDEYDVVII GGGASGLTAA SEFTHERVLV
LEKSSTFGGN ARYHTFNRLK HPTAGVCFQE PFPGSNMLRL LKKIGLEGKY KSNEKDTLVF
FDTFLLLKCL GEIVVGFIKQ PRYLLKLSVW GLTSQLFLHA IIGKPYVVAA KQLGDPIFAD
LYTFLDKFSP RGDFYPRLPW TPNGSWSKAH MELLDNISLY TYLFEPDKLG RLPEQLRPPA
RLGKLVENAV STTLRVECLD IHDVSAYVGL HFLVGYLRGN LVTLPGGNGS ISAGLCKYLS
HQRNVTLQNH VQLTAVEPQH NGTCIQFTIN GQPRQVQAQQ IIWAAPKTQL ATWLPGLPAK
QLAAIKNIRH EDYYLANVFL SKPVLGHSFG GYMIEPDSNK DPFSWCKAGT CLVANWMDDH
ADVDVGVLTL LKPTTRSERQ DRTAQNAFLA LQQQTYAEIA KVLRNIGIGA EVIEDIQIWY
WPAGLVTSVV GQQAEGVFET ARQSFENIHF ANQDSVGVGN IESAILSGID AANAVKAQLM
DTENVVEVAG