ID   PIGC_SERMA              Reviewed;         888 AA.
AC   Q5W252;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Prodigiosin synthesizing transferase PigC {ECO:0000303|PubMed:18401499};
DE            EC=6.4.-.- {ECO:0000305|PubMed:18401499};
DE   AltName: Full=Prodigiosin synthetase PigC {ECO:0000303|PubMed:18401499};
GN   Name=pigC {ECO:0000303|PubMed:15528645};
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 274 / NCDO 740 / NCIB 1377 / NCTC 1377;
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, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 274 / NCDO 740 / NCIB 1377 / NCTC 1377;
RX   PubMed=18401499; DOI=10.1039/b719353j;
RA   Chawrai S.R., Williamson N.R., Salmond G.P., Leeper F.J.;
RT   "Chemoenzymatic synthesis of prodigiosin analogues--exploring the substrate
RT   specificity of PigC.";
RL   Chem. Commun. (Camb.) 2008:1862-1864(2008).
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. It is able to use substrates with a variety of
CC       monocyclic rings in place of the pyrrolic ring A of its natural
CC       substrate. {ECO:0000269|PubMed:18401499}.
CC   -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC       {ECO:0000250|UniProtKB:Q5W269, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PigC family. {ECO:0000305}.
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DR   EMBL; AJ833002; CAH55648.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5W252; -.
DR   SMR; Q5W252; -.
DR   BioCyc; MetaCyc:MON-18836; -.
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; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA: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..888
FT                   /note="Prodigiosin synthesizing transferase PigC"
FT                   /id="PRO_0000436237"
SQ   SEQUENCE   888 AA;  99191 MW;  153E5F62C3FAF289 CRC64;
     MNPTLVVELS GDKTLEPHRL GGKAHSLNHL IHAGLPVPPA FCITAQAYRQ FIEFAVPGAL
     LDTGAPGNVR DMILSAAIPA PLDLAIRHAC KQLGDGASLA VRSSALEEDG LTHSFAGQYD
     TYLHVRGDDE VVRKVQSCWA SLWAERAAQY SRTSAAQSDI AVVLQIMVDA DAAGVMFTQD
     PLTGDANHIV IDSCWGLGEG VVSGQVTTDS FILDKASGEI RERQIRHKPH YCQRDPQGRV
     TLLQTPEARR DAPSLTPEQL QQLARLARQT RMIYGAELDI EWAVKDDRVW LLQARPITTQ
     AKPVQMLYAN PWESDPTIKE RAFFSRMDTG EIVTGLMTPL GLSFCQFYQK HIHGPAIKTM
     GLADIGDWQI YMGYLQGYVY LNISGSAYML RQCPPTRDEM KFTTRYATAD IDFSGYKNPY
     GPGVQGWAYL KSAWHWLKQQ RHNLRSAGAT VDAMIALRQR ETRRFLALDL TTMTHQELER
     ELSRIDGYFL DSCAAYMPFF LQSFALYDAL ALTCERYLKG RGNGLQNRIK ASMNNLRTIE
     VTLGILSLVE TVNRQPALKA LFERHSAQEL VTVLPTDPES RAFWQSDFSA FLFEFGARGR
     QEFELSLPRW NDDPSYLLQV MKMYLQHPVD LHTKLRETER LRHEDSAALL KAMPWFGRMK
     LKFITKLYGV MAERREATRP TFVTETWFYR RIMLEVLRRL EAQGLVKSAD LPYVDFERFR
     AFMAGEQSAQ EAFAADLIER NRHQHLLNLH AEEPPMAIVG GYQPRMKAPT AENAAGMLSG
     LAASPGKVVA KARVITDLLA QAGELQPNEI LVARFTDASW TPLFALAAGI VTDIGSALSH
     SCIVAREFGI PAAVNLKNAT QLINSGDTLI LDGDSGTVII QRGERADG