PDUD_CITFR
ID PDUD_CITFR Reviewed; 224 AA.
AC P0DUM8;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Propanediol dehydratase medium subunit;
DE EC=4.2.1.28 {ECO:0000305|PubMed:18332146};
DE AltName: Full=Diol dehydratase medium subunit {ECO:0000303|PubMed:18332146};
DE Short=DDH medium subunit;
DE AltName: Full=Propanediol utilization protein PduD;
GN Name=pduD {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, CATALYTIC ACTIVITY, 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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20417607; DOI=10.1016/j.molcel.2010.04.008;
RA Parsons J.B., Frank S., Bhella D., Liang M., Prentice M.B., Mulvihill D.P.,
RA Warren M.J.;
RT "Synthesis of empty bacterial microcompartments, directed organelle protein
RT incorporation, and evidence of filament-associated organelle movement.";
RL Mol. Cell 38:305-315(2010).
RN [3]
RP FUNCTION, SUBCELLULAR 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: Part of the PduCDE complex that catalyzes the dehydration of
CC 1,2-propanediol (1,2-PD) to propionaldehyde (Probable). This subunit is
CC directly targeted to the bacterial microcompartment (BMC)
CC (PubMed:20417607, PubMed:24933391). {ECO:0000269|PubMed:20417607,
CC ECO:0000269|PubMed:24933391, ECO:0000305|PubMed:18332146}.
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 BMCs in its cytoplasm. {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.
CC {ECO:0000305|PubMed:20417607}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=propane-1,2-diol = H2O + propanal; Xref=Rhea:RHEA:14569,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16997, ChEBI:CHEBI:17153; EC=4.2.1.28;
CC Evidence={ECO:0000305|PubMed:18332146};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000250|UniProtKB:O31041};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000269|PubMed:18332146}.
CC -!- SUBUNIT: The propanediol dehydratase enzyme is a heterotrimeric complex
CC composed of a large (PduC), a medium (PduD) and a small (PduE) subunit.
CC {ECO:0000250|UniProtKB:O31041}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:18332146, ECO:0000269|PubMed:20417607,
CC ECO:0000305|PubMed:24933391}. Note=Probably in the interior of the BMC.
CC {ECO:0000305|PubMed:20417607}.
CC -!- DOMAIN: The N-terminal 18 residues form an alpha-helix which targets
CC this enzyme and foreign proteins (tested with alcohol dehydrogenase) to
CC the BMC. {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 diol/glycerol dehydratase medium subunit
CC family. {ECO:0000305}.
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DR EMBL; AM498294; CAM57286.1; -; Genomic_DNA.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.10150; -; 1.
DR InterPro; IPR010254; B12-dep_deHydtase_bsu.
DR InterPro; IPR003208; Dehydtase/Dehydtase_re.
DR InterPro; IPR025541; Ppandiol/glycerol_DHydtase_msu.
DR Pfam; PF02288; Dehydratase_MU; 1.
DR PIRSF; PIRSF018506; Prpndl_dhdrts_md; 1.
DR SUPFAM; SSF52968; SSF52968; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Cobalamin; Cobalt; Lyase.
FT CHAIN 1..224
FT /note="Propanediol dehydratase medium subunit"
FT /id="PRO_0000454259"
FT REGION 1..18
FT /note="Targets protein to the BMC"
FT /evidence="ECO:0000269|PubMed:24933391"
SQ SEQUENCE 224 AA; 24281 MW; 743997FCD4D957C0 CRC64;
MEINEKLLRQ IIEDVLSEMQ TSDKPVSFRA STAASAPQAA AAQGDSFLTE IGEAKQGQQQ
DEVIIAVGPA FGLSQTVNIV GIPHKNILRE VIAGIEEEGI KARVIRCFKS SDVAFVAVEG
NRLSGSGISI GIQSKGTTVI HQQGLPPLSN LELFPQAPLL TLETYRQIGK NAARYAKRES
PQPVPTLNDQ MARPKYQAKS AILHIKETKY VVTGKNPQEL RVAL
