PDUP_SALTY
ID PDUP_SALTY Reviewed; 464 AA.
AC Q9XDN1; Q7BV76;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Propanal dehydrogenase (CoA-propanoylating);
DE EC=1.2.1.87 {ECO:0000269|PubMed:14504694};
DE AltName: Full=Coenzyme-A-acylating propionaldehyde dehydrogenase {ECO:0000303|PubMed:14504694};
DE AltName: Full=Propanediol utilization protein PduP;
GN Name=pduP {ECO:0000303|PubMed:10498708}; OrderedLocusNames=STM2051;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=10498708; DOI=10.1128/jb.181.19.5967-5975.1999;
RA Bobik T.A., Havemann G.D., Busch R.J., Williams D.S., Aldrich H.C.;
RT "The propanediol utilization (pdu) operon of Salmonella enterica serovar
RT typhimurium LT2 includes genes necessary for formation of polyhedral
RT organelles involved in coenzyme B(12)-dependent 1, 2-propanediol
RT degradation.";
RL J. Bacteriol. 181:5967-5975(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=12923081; DOI=10.1128/jb.185.17.5086-5095.2003;
RA Havemann G.D., Bobik T.A.;
RT "Protein content of polyhedral organelles involved in coenzyme B12-
RT dependent degradation of 1,2-propanediol in Salmonella enterica serovar
RT Typhimurium LT2.";
RL J. Bacteriol. 185:5086-5095(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=14504694; DOI=10.1007/s00203-003-0601-0;
RA Leal N.A., Havemann G.D., Bobik T.A.;
RT "PduP is a coenzyme-a-acylating propionaldehyde dehydrogenase associated
RT with the polyhedral bodies involved in B12-dependent 1,2-propanediol
RT degradation by Salmonella enterica serovar Typhimurium LT2.";
RL Arch. Microbiol. 180:353-361(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA Penrod J.T., Roth J.R.;
RT "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT in Salmonella enterica.";
RL J. Bacteriol. 188:2865-2874(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 1-MET--ILE-10
RP AND 1-MET--LEU-14.
RC STRAIN=LT2;
RX PubMed=20308536; DOI=10.1073/pnas.0913199107;
RA Fan C., Cheng S., Liu Y., Escobar C.M., Crowley C.S., Jefferson R.E.,
RA Yeates T.O., Bobik T.A.;
RT "Short N-terminal sequences package proteins into bacterial
RT microcompartments.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7509-7514(2010).
RN [7]
RP FUNCTION, INTERACTION WITH PDUA AND PDUJ, DOMAIN, AND MUTAGENESIS OF
RP 2-ASN--LEU-18; GLU-7; ILE-10 AND LEU-14.
RC STRAIN=LT2;
RX PubMed=22927404; DOI=10.1073/pnas.1207516109;
RA Fan C., Cheng S., Sinha S., Bobik T.A.;
RT "Interactions between the termini of lumen enzymes and shell proteins
RT mediate enzyme encapsulation into bacterial microcompartments.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:14995-15000(2012).
RN [8]
RP FUNCTION, INTERACTION WITH PDUQ, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=23077559; DOI=10.1371/journal.pone.0047144;
RA Cheng S., Fan C., Sinha S., Bobik T.A.;
RT "The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+
RT internally within the Pdu microcompartment of Salmonella enterica.";
RL PLoS ONE 7:e47144-e47144(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=LT2;
RX PubMed=26283792; DOI=10.1074/jbc.m115.651919;
RA Jakobson C.M., Kim E.Y., Slininger M.F., Chien A., Tullman-Ercek D.;
RT "Localization of proteins to the 1,2-propanediol utilization
RT microcompartment by non-native signal sequences is mediated by a common
RT hydrophobic motif.";
RL J. Biol. Chem. 290:24519-24533(2015).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=27063436; DOI=10.1038/srep24359;
RA Held M., Kolb A., Perdue S., Hsu S.Y., Bloch S.E., Quin M.B.,
RA Schmidt-Dannert C.;
RT "Engineering formation of multiple recombinant Eut protein nanocompartments
RT in E. coli.";
RL Sci. Rep. 6:24359-24359(2016).
RN [11]
RP SYSTEM-MODELING, AND FUNCTION.
RC STRAIN=LT2;
RX PubMed=28475631; DOI=10.1371/journal.pcbi.1005525;
RA Jakobson C.M., Tullman-Ercek D., Slininger M.F., Mangan N.M.;
RT "A systems-level model reveals that 1,2-Propanediol utilization
RT microcompartments enhance pathway flux through intermediate
RT sequestration.";
RL PLoS Comput. Biol. 13:e1005525-e1005525(2017).
CC -!- FUNCTION: A CoA-acylating aldehyde dehydrogenase required for optimal
CC 1,2-propanediol (1,2-PD) degradation (PubMed:14504694,
CC PubMed:20308536). Optimizes growth in the bacterial microcompartment
CC (BMC) dedicated to 1,2-PD degradation by minimizing propionaldehyde
CC toxicity (Probable). Directly targeted to the BMC (PubMed:20308536,
CC PubMed:22927404, PubMed:26283792). NAD(+) and NADH are regenerated
CC internally within the Pdu BMC by the PduP and PduQ enzymes, which
CC reduce NAD(+) and oxidize NADH respectively, although there must also
CC be cofactor transport across the BMC (PubMed:23077559).
CC {ECO:0000269|PubMed:14504694, ECO:0000269|PubMed:20308536,
CC ECO:0000269|PubMed:22927404, ECO:0000269|PubMed:23077559,
CC ECO:0000269|PubMed:26283792, ECO:0000305|PubMed:20308536}.
CC -!- FUNCTION: The 1,2-PD-specific bacterial microcompartment (BMC)
CC concentrates low levels of 1,2-PD catabolic enzymes, concentrates
CC volatile reaction intermediates thus enhancing pathway flux and keeps
CC the level of toxic, mutagenic propionaldehyde low.
CC {ECO:0000305|PubMed:28475631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + NAD(+) + propanal = H(+) + NADH + propanoyl-CoA;
CC Xref=Rhea:RHEA:36027, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.87;
CC Evidence={ECO:0000269|PubMed:14504694};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000305|PubMed:10498708}.
CC -!- SUBUNIT: Interacts with BMC shell proteins PduA and PduJ, which target
CC this protein to BMC (PubMed:22927404). Interacts with PduQ, probably
CC via the N-terminus of PduQ (PubMed:23077559). Interacts with PduK,
CC probably with its BMC-containing N-terminus (By similarity).
CC {ECO:0000250|UniProtKB:B1VB75, ECO:0000269|PubMed:22927404,
CC ECO:0000269|PubMed:23077559}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:14504694, ECO:0000269|PubMed:20308536,
CC ECO:0000269|PubMed:26283792, ECO:0000269|PubMed:27063436,
CC ECO:0000305|PubMed:12923081, ECO:0000305|PubMed:23077559}.
CC Note=Probably located inside the BMC shell.
CC {ECO:0000305|PubMed:20308536}.
CC -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC medium. {ECO:0000269|PubMed:10498708}.
CC -!- DOMAIN: A short N-terminal, probably helical sequence targets this
CC enzyme and foreign proteins (tested with GST, MBP and eGFP) to the BMC.
CC 10 residues give poor localization while 14 is better and 18 is better
CC yet. The cargo is only detected by Western blot in broken shells,
CC strongly suggesting this protein is normally found inside the BMC and
CC not on its exterior (PubMed:20308536, PubMed:22927404,
CC PubMed:26283792). This N-terminal sequence interacts with the C-
CC terminus of PduA, and possibly also with PduJ, to encapsulate PduP into
CC BMCs (PubMed:22927404). PduD and PduP compete for encapsulation in BMCs
CC (PubMed:26283792). {ECO:0000269|PubMed:20308536,
CC ECO:0000269|PubMed:22927404, ECO:0000269|PubMed:26283792}.
CC -!- DISRUPTION PHENOTYPE: Significantly impaired for growth on 1,2-PD/CN-
CC B12, loss of propionaldehyde dehydrogenase activity (PubMed:14504694).
CC Releases decreased amounts of acetaldehyde when grown on propanediol
CC (PubMed:16585748). {ECO:0000269|PubMed:14504694,
CC ECO:0000269|PubMed:16585748}.
CC -!- MISCELLANEOUS: Bacterial microcompartments (BMC) 100-200 nm in cross
CC section are formed during aerobic growth on minimal 1,2-PD-B12 or
CC anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic
CC growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate
CC (PubMed:10498708). BMCs can constitute up to 10% of total cell protein
CC (PubMed:12923081). {ECO:0000269|PubMed:10498708,
CC ECO:0000269|PubMed:12923081}.
CC -!- SIMILARITY: Belongs to the EutE/PduP family. {ECO:0000305}.
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DR EMBL; AF026270; AAD39015.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20955.1; -; Genomic_DNA.
DR RefSeq; NP_460996.1; NC_003197.2.
DR RefSeq; WP_001097680.1; NC_003197.2.
DR AlphaFoldDB; Q9XDN1; -.
DR SMR; Q9XDN1; -.
DR STRING; 99287.STM2051; -.
DR PaxDb; Q9XDN1; -.
DR EnsemblBacteria; AAL20955; AAL20955; STM2051.
DR GeneID; 1253572; -.
DR KEGG; stm:STM2051; -.
DR PATRIC; fig|99287.12.peg.2173; -.
DR HOGENOM; CLU_028794_1_0_6; -.
DR OMA; TCEQLMP; -.
DR PhylomeDB; Q9XDN1; -.
DR BioCyc; MetaCyc:STM2051-MON; -.
DR BioCyc; SENT99287:STM2051-MON; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031472; C:propanediol degradation polyhedral organelle; IDA:UniProtKB.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:InterPro.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07121; ALDH_EutE; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR012408; Acetald_propionald_DH-rel.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036410; EutE_PduP; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..464
FT /note="Propanal dehydrogenase (CoA-propanoylating)"
FT /id="PRO_0000454280"
FT REGION 1..18
FT /note="Targets protein to the BMC"
FT /evidence="ECO:0000269|PubMed:20308536"
FT MUTAGEN 1..14
FT /note="Missing: Much less protein associates with BMCs, no
FT effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:20308536"
FT MUTAGEN 1..10
FT /note="Missing: Much less protein associates with BMCs, no
FT effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:20308536"
FT MUTAGEN 2..18
FT /note="Missing: No longer interacts with PduA."
FT /evidence="ECO:0000269|PubMed:22927404"
FT MUTAGEN 7
FT /note="E->A: Substantially decreased protein levels in
FT BMCs, no change in enzyme activity."
FT /evidence="ECO:0000269|PubMed:22927404"
FT MUTAGEN 10
FT /note="I->A: Substantially decreased protein levels in
FT BMCs, no change in enzyme activity."
FT /evidence="ECO:0000269|PubMed:22927404"
FT MUTAGEN 14
FT /note="L->A: Substantially decreased protein levels in
FT BMCs, no change in enzyme activity."
FT /evidence="ECO:0000269|PubMed:22927404"
SQ SEQUENCE 464 AA; 49046 MW; 9D5774630A525534 CRC64;
MNTSELETLI RTILSEQLTT PAQTPVQPQG KGIFQSVSEA IDAAHQAFLR YQQCPLKTRS
AIISAMRQEL TPLLAPLAEE SANETGMGNK EDKFLKNKAA LDNTPGVEDL TTTALTGDGG
MVLFEYSPFG VIGSVAPSTN PTETIINNSI SMLAAGNSIY FSPHPGAKKV SLKLISLIEE
IAFRCCGIRN LVVTVAEPTF EATQQMMAHP RIAVLAITGG PGIVAMGMKS GKKVIGAGAG
NPPCIVDETA DLVKAAEDII NGASFDYNLP CIAEKSLIVV ESVAERLVQQ MQTFGALLLS
PADTDKLRAV CLPEGQANKK LVGKSPSAML EAAGIAVPAK APRLLIALVN ADDPWVTSEQ
LMPMLPVVKV SDFDSALALA LKVEEGLHHT AIMHSQNVSR LNLAARTLQT SIFVKNGPSY
AGIGVGGEGF TTFTIATPTG EGTTSARTFA RSRRCVLTNG FSIR
