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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}.
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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
 
 
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