ID   PIGD_SERMA              Reviewed;         904 AA.
AC   Q5W251;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Thiamine diphosphate dependent-3-acetyloctanal synthase PigD {ECO:0000305};
DE            Short=ThDP-dependent enzyme PigD {ECO:0000303|PubMed:20669204};
DE            EC=2.2.1.12 {ECO:0000269|PubMed:20669204};
GN   Name=pigD {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, COFACTOR, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 274 / NCDO 740 / NCIB 1377 / NCTC 1377;
RX   PubMed=20669204; DOI=10.1002/anie.201000632;
RA   Dresen C., Richter M., Pohl M., Luedeke S., Mueller M.;
RT   "The enzymatic asymmetric conjugate umpolung reaction.";
RL   Angew. Chem. Int. Ed. 49:6600-6603(2010).
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. In vitro, it can act on a
CC       number of alpha,beta-unsaturated carbonyl compounds, including
CC       aldehydes and ketones, and can catalyze both 1,2-addition and Stetter-
CC       type 1,4-addition depending on the substrate.
CC       {ECO:0000269|PubMed:20669204}.
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:0000269|PubMed:20669204};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:20669204};
CC   -!- PATHWAY: Antibiotic biosynthesis; prodigiosin biosynthesis.
CC       {ECO:0000250|UniProtKB:Q5W268, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; AJ833002; CAH55649.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5W251; -.
DR   SMR; Q5W251; -.
DR   BioCyc; MetaCyc:MON-18822; -.
DR   BRENDA; 2.2.1.12; 5690.
DR   UniPathway; UPA01072; -.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:UniProtKB.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR029061; THDP-binding.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..904
FT                   /note="Thiamine diphosphate dependent-3-acetyloctanal
FT                   synthase PigD"
FT                   /id="PRO_0000436239"
FT   REGION          879..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..904
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  101200 MW;  50871B3C4A48BF53 CRC64;
     MRAATAACRD RRGLCRAEFA RLAEAVTPFW LHKELIMTTL TGQARLTNSA AYEQVWQAER
     QACRTDADPD TLTVGVVVVT RNPAFFQTGL SVLNDIRDYV FNRVHIQSEM PLKLLDLAAD
     SLYLAAREKA LHFLKGQNKA INVRIIQCAS LAEATGKIIY THALEQRPEF HLGMLFYDQT
     TPAGVDDSIE QIDRDLDAFY SALQRSGIPA FYTTFSTVAF IRQLRSPFRY LPQQYREIVR
     SEDPAIFQTE LLCLWMDFFE MNYTNRRVKP IGALALHNTL GEQLIQFFER TAAERWLVSY
     YTGSIISNLI GYLDRHAEAR GALILRGPNE HAIACGAMAN WQLYRMPFLG VVTSGMMDEF
     KGTLANLKET AAQGIIVAAE NRGNQWYSFQ GTLTPTEDMR EVLIARRIPF VYIDDVEMIG
     AGLTEAFRLY HQGQGPVVIL ATQNVLESTL SLEGAVCDPS PIPVLSADDP LPMSESLAQA
     IALINRGPER LVWQLGPVSD DEYALIHDIA DAAGIALVDS LAHPGSAPKY YQGRRNPHYL
     GTLAIYGYSP RVYNFLHTND KLNAMSEQSL FMIKSRVAQI TTPFSDGRLE RKVHLVQLTH
     DDRHLSAYAD LHLHMNCLAF LRTVKAHLDV DPALRERRRA LIAAYLDSPS DVVSQLPSLP
     MSANYFFCQL NRVIEELIET EGFDFTGVYD VGRCGISAAR NVAKTRRGFS GWYGRALMGD
     ALLATGYLAY TSPSHVMAFI GDGAKGIVPD ILPAFIDNIL THPQLLNKSI TVFYLCNGGL
     SVINTYQERI LFNRTSRQMR LVNVEQPDVE QTVNNFHIQS KTLTHFDEDV IRQALTTSHR
     LNLFSVVLGH NNEGDGISPG HRQRLAALIR ADHDALQERK AWAAQQPEST STAFDQDPTQ
     EATS