ID   PDUC_CITFR              Reviewed;         554 AA.
AC   P0DUM7;
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 large subunit;
DE            EC=4.2.1.28 {ECO:0000305|PubMed:18332146};
DE   AltName: Full=Diol dehydratase large subunit {ECO:0000303|PubMed:18332146};
DE            Short=DDH large subunit;
DE   AltName: Full=Propanediol utilization protein PduC;
GN   Name=pduC {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).
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). {ECO:0000269|PubMed:20417607,
CC       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:P37450};
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:P37450}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000269|PubMed:18332146, ECO:0000269|PubMed:20417607}.
CC       Note=Probably in the interior of the BMC.
CC       {ECO:0000305|PubMed:20417607}.
CC   -!- SIMILARITY: Belongs to the diol/glycerol dehydratase large subunit
CC       family. {ECO:0000255|PIRNR:PIRNR018507}.
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DR   EMBL; AM498294; CAM57285.1; -; 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   CDD; cd03687; Dehydratase_LU; 1.
DR   Gene3D; 3.20.20.350; -; 1.
DR   InterPro; IPR016176; Cbl-dep_enz_cat.
DR   InterPro; IPR036999; Diol/glycerol_deHase_lsu_sf.
DR   InterPro; IPR003206; Diol/glycerol_deHydtase_lsu.
DR   Pfam; PF02286; Dehydratase_LU; 1.
DR   PIRSF; PIRSF018507; Prpndl_dhdrts_lg; 1.
DR   SUPFAM; SSF51703; SSF51703; 1.
PE   1: Evidence at protein level;
KW   Bacterial microcompartment; Cobalamin; Cobalt; Lyase.
FT   CHAIN           1..554
FT                   /note="Propanediol dehydratase large subunit"
FT                   /id="PRO_0000454258"
SQ   SEQUENCE   554 AA;  60280 MW;  711071A46EE62CF4 CRC64;
     MRSKRFEALA KRPVNQDGFV KEWIEEGFIA MESPNDPKPS IKIVNGTVTE LDGKSASEFD
     LIDHFIARYG INLARAEEVM AMDSVKLANM LCDPNVKRKD IVPLTTAMTP AKIVEVVSHM
     NVVEMMMAMQ KMRARRTPSQ QAHVTNVKDN PVQIAADAAE GAWRGFDEQE TTVAVARYAP
     FNAIALLVGS QVGRPGVLTQ CSLEEATELK LGMLGHTCYA ETISVYGTEP VFTDGDDTPW
     SKGFLASSYA SRGLKMRFTS GSGSEVQMGY AEGKSMLYLE ARCIYITKAA GVQGLQNGSV
     SCIGVPSAVP SGIRAVLAEN LICSSLDLEC ASSNDQTFTH SDMRRTARLL MQFLPGTDFI
     SSGYSAVPNY DNMFAGSNED AEDFDDYNVL QRDLKVDGGL RPVREEDVIA IRNKAARALQ
     AVFAGMGLPP ITDEEVEAAT YAHGSKDMPE RNIVEDIKFA QEIINKNRNG LEVVKALAQG
     GFTDVAQDML NIQKAKLTGD YLHTSAIIVG DGQVLSAVND VNDYAGPATG YRLQGERWEE
     IKNIPGALDP NELG