ID   PIGC_SERS3              Reviewed;         890 AA.
AC   Q5W269;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Prodigiosin synthesizing transferase PigC {ECO:0000303|PubMed:15853884};
DE            EC=6.4.-.- {ECO:0000305|PubMed:15853884};
DE   AltName: Full=Prodigiosin synthetase PigC {ECO:0000303|PubMed:15853884};
GN   Name=pigC {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, 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 transfer of 2-methyl-3-
CC       n-amyl-pyrrole (MAP) to 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC)
CC       to yield prodigiosin. {ECO:0000269|PubMed:15853884}.
CC   -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC       {ECO:0000305|PubMed:15853884}.
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), 4-hydroxy-2,2'-bipyrrole-5-
CC       methanol (HBM) and 2-methyl-3-n-amyl-pyrrole (MAP).
CC       {ECO:0000269|PubMed:15853884}.
CC   -!- MISCELLANEOUS: The mechanism for the condensation reaction is that a
CC       phosphoryl group from ATP is transferred via His-840 in the C-terminal
CC       phosphoryl transfer domain to the oxygen atom of the aldehyde group of
CC       MBC. This exposes the otherwise fairly unreactive aldehyde to
CC       modification by the C-5 of MAP. After this initial formation of the C-C
CC       bond, the loss of the proton from what had been C-5 of MAP and the
CC       elimination of phosphate is possible. {ECO:0000305|PubMed:15853884}.
CC   -!- SIMILARITY: Belongs to the PigC family. {ECO:0000305}.
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DR   EMBL; AJ833001; CAH55631.1; -; Genomic_DNA.
DR   RefSeq; WP_021014641.1; NZ_CP025085.1.
DR   AlphaFoldDB; Q5W269; -.
DR   SMR; Q5W269; -.
DR   STRING; 104623.Ser39006_01371; -.
DR   KEGG; ag:CAH55631; -.
DR   eggNOG; COG0574; Bacteria.
DR   eggNOG; COG3848; Bacteria.
DR   OrthoDB; 997616at2; -.
DR   UniPathway; UPA01072; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IMP:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..890
FT                   /note="Prodigiosin synthesizing transferase PigC"
FT                   /id="PRO_0000436238"
SQ   SEQUENCE   890 AA;  99766 MW;  13973C2CA89B9BA5 CRC64;
     MNQPLVVEIS GDKALEHHHL GGKGYSLNNL IHAGLPVPSA FCVTAQAYQQ FIEEVVPGAE
     LTDGDLIAVR DAILHADIPD SLKQAIGDAY QHLGHDTTIA VRSSALDEDG QRQSFAGQYE
     TYLHVKGSEA VLHKVQACWA SLWAERAAQY RHESASHSAI AVILQVMVDA DAAGVMFTQD
     PLSGSTDKVV IDSCWGLGEG VVSGQVTTDS FTLDKATGEL CDQQIRHKPN YCQRDEHGLV
     TLLQTPEAKR DLPSLTPAQL QQLVTLARQA QLIYSTELDI EWAVKDDKVW LLQARPVTTS
     AKTANVIYAN PWESDPAAKE GAFFSRMDTG EIVTGLMTPL GLSFCQFYQK HIHGPAIKTM
     GLADISHWQI YMGYIQGYVY LNISGSAYML RQCPPTRNEM KFTTRYATDE IDFKDYKNPY
     GAGVQGWDYA KSCWYWLKQQ VRNMRSAART VEQMIALRQD ETTRFLGLDL TAMTLQQLDQ
     ELQRIDRFFL DSCAAYMPFF LQSFALYDAL AQACERHIKD GKGLQNRIKA SMNNLRTIEV
     TLGIIKLVAT VNQQTELKAL FEQHRADELV TLLPVHDISR AFWQGDFEDF LVEFGSRGRQ
     EFDLSIPRWR DDPSYLLQVM KMYLQHPVDL HKKLRETELL RQQDSEALFS AMSWSGRFKL
     KTLIKLYGMM AERREATRPT FITETWFYRC IMLEVLRRLD AQGIASSADL PYVDFEQFRA
     YVAGTIPAEQ AFSKARLDQN RHQHLFNLHA EEPPMAIVGP YTPKVKAPTQ DDKTIRSLTG
     LAASPGNVVA KARVITDLQV QAGEFQPDEI LVARFTDASW TPLFALAAGI VTDIGSTLSH
     SCIVAREFGI PAVVNLKTAT QIINSGDMLI LDGDSGTVII QHQEERNHDG