PIGJ_SERS3
ID PIGJ_SERS3 Reviewed; 770 AA.
AC Q5W262;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Beta-ketoacyl synthase PigJ {ECO:0000303|PubMed:17002325};
DE Short=PKS {ECO:0000303|PubMed:17002325};
DE EC=2.3.1.- {ECO:0000305|PubMed:15853884, ECO:0000305|PubMed:17002325};
GN Name=pigJ {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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DOMAIN.
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 decarboxylation on the malonyl group attached to PigH to yield a C2
CC carbanion of acetyl-S-PigH. Then, the heterocyclic pyrrole group of
CC PigG moves to the PigJ active site Cys-525 to generate a transient
CC pyrrolyl-S-cysteinyl PigJ intermediate (acyl donor) whose pyrrolyl
CC group is captured by the C2 carbanion of acetyl-S-PigH to yield the
CC pyrrolyl-beta-ketoacyl-S-PigH. {ECO:0000269|PubMed:15853884,
CC ECO:0000269|PubMed:17002325}.
CC -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC {ECO:0000305|PubMed:15853884, ECO:0000305|PubMed:17002325}.
CC -!- DOMAIN: It seems that PigJ is composed by an active ketosynthase (KS)
CC domain and by a chain length factor (CLF) partner domain that
CC potentially decarboxylates the malonyl group of PigH.
CC {ECO:0000305|PubMed:17002325}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a white phenotype
CC and produce 2-methyl-3-n-amyl-pyrrole (MAP).
CC {ECO:0000269|PubMed:15853884}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; AJ833001; CAH55638.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5W262; -.
DR SMR; Q5W262; -.
DR STRING; 104623.Ser39006_01378; -.
DR KEGG; ag:CAH55638; -.
DR eggNOG; COG3321; Bacteria.
DR UniPathway; UPA01072; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; SSF53901; 3.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic biosynthesis; Transferase.
FT CHAIN 1..770
FT /note="Beta-ketoacyl synthase PigJ"
FT /id="PRO_0000436247"
FT ACT_SITE 525
FT /evidence="ECO:0000250|UniProtKB:P9WQD9"
FT BINDING 652
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQD9"
FT BINDING 690
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WQD9"
SQ SEQUENCE 770 AA; 83742 MW; 89C02E13CA936E33 CRC64;
MSNDKHIAPL AVVSMGCVLP GVDHFRALDT IADWETVFQS ASPLAWSETS RPIQGRQMDD
SGFDFKKFSI PPLFRKAVSR ETRLALRAAE DALAGLVLPE SLRDCCDQFC AIHLGSDAAY
RNATKVGALR ALAEKLQAQG CPAAEVRRRL DDYKQPLAES LGCSSHDRVG EMASSIPARI
AHFAHTRGKC QTLDGADKGG LRLLQLAQDC FRYHDSQMAV LTSVQCFHHR PQAYMLLEQG
VSQDACWLEG AISLVVCPLA VAHEQGWPVL TQLGDIVTTH DGSPQPEADH PAALYFAGAN
QVFCQIVEMV LRQHQRCEGR SFTGGRWQVN VAQTQSLTPA VDDRVAIVDY QPITGHPLDK
TQFWQTLEQG EDALREHSAA HVNAEAFVRT TQQKLSTYIH RTMSFPAHSP SDVALKKPMM
PAKKQRLDVT QLYALNSCHS WSEKIRQFER VAIIIASNLS LSADRLQAMR ALWSGLPGSE
GAIPLPELPS INHWSWYGAC GIGTAQLLAQ YFGISADCYA VEAACASSLA AVHDAVRALQ
AGRYDAVIVG GIETATLERD LVLCSAQMML SVSRIRPFSQ GADGFTPGDG GGFVMLTHHP
VPRAIATIEA ISGSCDSYSM TAPDPLGQAL AIKKTLSLTA IDAQTVQYLE AHGTGTELGD
RSEVMSLKYS YHRDKHSPLY IGSAKYNFGH CFAGAGALSL CKVLSAFEHE RIPPTPVSEL
NVDLPLGDIP AEVPQQAIPW RLSEDGQRKA AINAFGTGGI NYHLVIRQSS
