PDUP_CITFR
ID PDUP_CITFR Reviewed; 461 AA.
AC B1VB75;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Propanal dehydrogenase (CoA-propanoylating);
DE EC=1.2.1.87 {ECO:0000250|UniProtKB:Q9XDN1};
DE AltName: Full=Coenzyme-A-acylating propionaldehyde dehydrogenase {ECO:0000303|PubMed:18332146};
DE AltName: Full=Propanediol utilization protein PduP;
GN Name=pduP {ECO:0000303|PubMed:18332146};
OS Citrobacter freundii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=546;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION BY MASS
RP SPECTROMETRY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT "Biochemical and Structural Insights into Bacterial Organelle Form and
RT Biogenesis.";
RL J. Biol. Chem. 283:14366-14375(2008).
RN [2]
RP STRUCTURE BY NMR OF 1-18, FUNCTION, INTERACTION WITH PDUK, SUBCELLULAR
RP LOCATION, DOMAIN, AND BIOTECHNOLOGY.
RX PubMed=24933391; DOI=10.1021/sb4001118;
RA Lawrence A.D., Frank S., Newnham S., Lee M.J., Brown I.R., Xue W.F.,
RA Rowe M.L., Mulvihill D.P., Prentice M.B., Howard M.J., Warren M.J.;
RT "Solution structure of a bacterial microcompartment targeting peptide and
RT its application in the construction of an ethanol bioreactor.";
RL ACS Synth. Biol. 3:454-465(2014).
CC -!- FUNCTION: A CoA-acylating aldehyde dehydrogenase required for optimal
CC 1,2-propanediol (1,2-PD) degradation. Optimizes growth in the bacterial
CC microcompartment (BMC) dedicated to 1,2-PD degradation by minimizing
CC propionaldehyde toxicity. NAD(+) and NADH are regenerated internally
CC within the Pdu BMC by the PduP and PduQ enzymes, which reduce NAD(+)
CC and oxidize NADH respectively, although there must also be cofactor
CC transport across the BMC (By similarity). Directly targeted to the BMC
CC (PubMed:24933391). {ECO:0000250|UniProtKB:Q9XDN1,
CC ECO:0000269|PubMed:24933391}.
CC -!- FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon
CC in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the
CC appearance of bacterial microcompartments (BMC) in its cytoplasm.
CC {ECO:0000269|PubMed:18332146}.
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. {ECO:0000305}.
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:0000250|UniProtKB:Q9XDN1};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:18332146}.
CC -!- SUBUNIT: Interacts with PduK, probably with its BMC-containing N-
CC terminus (PubMed:24933391). Interacts with shell proteins PduA and
CC PduJ, interacts with PduQ (By similarity).
CC {ECO:0000250|UniProtKB:Q9XDN1, ECO:0000269|PubMed:24933391}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:18332146, ECO:0000305|PubMed:24933391}.
CC -!- DOMAIN: The N-terminal 18 residues form an alpha-helix which targets
CC this enzyme and foreign proteins (tested with mCherry, pea ascorbate
CC peroxidase and pyruvate decarboxylase) to the BMC.
CC {ECO:0000269|PubMed:24933391}.
CC -!- BIOTECHNOLOGY: Ethanogenic BMCs can be made in E.coli by targeting
CC pyruvate decarboxylase (pdc) and alcohol dehydrogenase (adh) to them.
CC PduP(1-18)-Pdc and PduD(1-18)-Adh strains targeted to the BMC (PduA,
CC PduB, PduJ, PduK, PduN, PduU) make significantly more ethanol than
CC strains where Pdc and Adh are not targeted to the BMC.
CC {ECO:0000269|PubMed:24933391}.
CC -!- SIMILARITY: Belongs to the EutE/PduP family. {ECO:0000305}.
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DR EMBL; AM498294; CAM57296.1; -; Genomic_DNA.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
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.
FT CHAIN 1..461
FT /note="Propanal dehydrogenase (CoA-propanoylating)"
FT /id="PRO_0000454279"
FT REGION 1..18
FT /note="Targets protein to the BMC"
FT /evidence="ECO:0000269|PubMed:24933391"
SQ SEQUENCE 461 AA; 48671 MW; 4CF6376EF53DF95C CRC64;
MNTSELETLI RNILSEQLAP AKAEVKGNGI FPSVSEAIDA AHQAFLRYQQ CPLKTRSAII
NALREELTPH LASLAAESAA ETGMGNKEDK FLKNKAALDN TPGIEDLTTT ALTGDGGMVL
FEYSPFGVIG SVAPSTNPTE TIINNSISML AAGNSVYFSP HPGAKAVSLK LITMIEDIAF
RCCGIRNLVV TVTEPTFEAT QQMMAHPKIA VLAITGGPGI VAMGMKSGKK VIGAGAGNPP
CIVDETADLV KAAEDIINGA SFDFNLPCIA EKSLIVVDAV AERLVQQMQS FGAMRLNSEE
IDKLRAVCLP EGIANKQLVG KSPATLLEAA GIPVPAKAPR LLIGIVKADD PWVTSEQLMP
MLPIVTVSDF DSALTLALKV EEGLHHTAIM HSQNVSRLNL AARTLQTSIF VKNGPSYAGI
GVGGEGFTTF TIATPTGEGT TSARTFARSR RCVLTNGFSI R
