ID   PIGD_SERS3              Reviewed;         866 AA.
AC   Q5W268;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Thiamine diphosphate dependent-3-acetyloctanal synthase PigD {ECO:0000305};
DE            Short=ThDP-dependent enzyme PigD {ECO:0000250|UniProtKB:Q5W251};
DE            EC=2.2.1.12 {ECO:0000250|UniProtKB:Q5W251};
DE   AltName: Full=Terminal condensing enzyme {ECO:0000303|PubMed:15853884};
GN   Name=pigD {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, 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 decarboxylation of
CC       pyruvate, followed by the modification of the resulting two-carbon
CC       fragment acetaldehyde at the C3 position of the 2-octenal (1,2-addition
CC       of acetaldehyde) giving 3-acetyloctanal. {ECO:0000269|PubMed:15853884}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octenal + H(+) + pyruvate = (S)-3-acetyloctanal + CO2;
CC         Xref=Rhea:RHEA:42832, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:61748, ChEBI:CHEBI:82759; EC=2.2.1.12;
CC         Evidence={ECO:0000250|UniProtKB:Q5W251};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:Q5W251};
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) and 4-hydroxy-2,2'-bipyrrole-5-
CC       methanol (HBM). {ECO:0000269|PubMed:15853884}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AJ833001; CAH55632.1; -; Genomic_DNA.
DR   RefSeq; WP_021014642.1; NZ_CP025085.1.
DR   AlphaFoldDB; Q5W268; -.
DR   SMR; Q5W268; -.
DR   STRING; 104623.Ser39006_01372; -.
DR   KEGG; ag:CAH55632; -.
DR   eggNOG; COG0028; Bacteria.
DR   OrthoDB; 85799at2; -.
DR   UniPathway; UPA01072; -.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; ISS:UniProtKB.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; ISS:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..866
FT                   /note="Thiamine diphosphate dependent-3-acetyloctanal
FT                   synthase PigD"
FT                   /id="PRO_0000436240"
FT   REGION          826..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   866 AA;  96977 MW;  66506324F1C7B04D CRC64;
     MTTMIGQTRQ AGSSSYEQAW QAEQAPCPGM EPDTLTVGVV VVTRNPTFFQ TGLSVLNDIR
     DYVFNRVHIQ SELPLKLSEL ASDPLYSEAR EKAIHFLKNQ SKALNIQVIQ CASLAEATGK
     IIYTHALEQQ PEFQMGMLFY DQTSLGNVDD SIEKIDRDLD AFYSAMQRGG IPAFYTTFST
     VTFIRDVRSS FRYLPQQYRE IVRSEDPAIF QTELLCLWMD FFEMNYTNRR VKPIGALALH
     NTLAEQLIQF FERTAASRWL VSYYTGSIIS NLIGYLDRHA EAHGALVLRG PNEHAIACGA
     MANWQLYRMP FLGVVTSGMM DEFKGTLINL KETAAQGIIV AAENRNNQWY SFQGTQTPTE
     DMRDVLAAKR IPYVYIDDVD GIADGLAEVF RLYHQAQGPV VILATQNVLE STLSLEPVPG
     DLPPVSGLPA YDCPPISDSF EQAMALINEG PEKLVWQLGP VSDDEYALVH EIADAAGLAL
     VDSLAHPGSA PKYYQGKRNP HYLGTLAIYG YSPRVYNFLH TNDKLNPMSD QSVFMIKSRV
     AQITTPFSDG RLERKVHLVQ LTHDERHLSP YADLKLHMDC LTFLRAVKAN LHVDAALREK
     RKALIAAYLD SPSDVVSQLP SLPMSANYFF CQLNRVIENL IKTENFDFTG VYDVGRCGIS
     AVRNVAKTRR GFSGWYGRAL MGDALLATSY LAHTSPTHVV AFIGDGAKGI VPDILPAFID
     NILTHPQLLN KSITIFYFCN GGLSVINTYQ ERILFNRTSR QMRLVNVDQP AFEQTVDDFH
     IQGKTLTHFD EDTIRHALMT PKRLNLFSVV LGHNNEGDGI SLATAKGWQR DPSDREALQE
     RKDWAARQPE STSTSFDQGQ NKEAIS