ID   PDUE_CITFR              Reviewed;         172 AA.
AC   P0DUM9;
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 small subunit;
DE            EC=4.2.1.28 {ECO:0000305|PubMed:18332146};
DE   AltName: Full=Diol dehydratase small subunit {ECO:0000303|PubMed:18332146};
DE            Short=DDH small subunit;
DE   AltName: Full=Propanediol utilization protein PduE;
GN   Name=pduE {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).
CC   -!- FUNCTION: Part of the PduCDE complex that catalyzes the dehydration of
CC       1,2-propanediol (1,2-PD) to propionaldehyde. Localized in the bacterial
CC       microcompartment (BMC) dedicated to 1,2-PD degradation.
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. {ECO:0000305}.
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:O31042};
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:O31042}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- SIMILARITY: Belongs to the diol/glycerol dehydratase small subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AM498294; CAM57287.1; -; 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; 1.10.1510.20; -; 1.
DR   InterPro; IPR003207; Ppandiol/glycerol_DeHydtase_su.
DR   InterPro; IPR036091; Prodiol/glycerol_DeHase__sf_su.
DR   Pfam; PF02287; Dehydratase_SU; 1.
DR   PIRSF; PIRSF018505; Prpndl_dhdrts_sm; 1.
DR   SUPFAM; SSF47148; SSF47148; 1.
PE   1: Evidence at protein level;
KW   Bacterial microcompartment; Cobalamin; Cobalt; Lyase.
FT   CHAIN           1..172
FT                   /note="Propanediol dehydratase small subunit"
FT                   /id="PRO_0000454260"
SQ   SEQUENCE   172 AA;  19234 MW;  9A647FEC51212DF7 CRC64;
     MNTDAIESMV RDVLSRMNSL QGESATPVAA SSSAHTAKVT DYPLANKHPE WVKTATNKTL
     DDFTLENVLS NKVTAQDMRI TPETLRLQAE IAKDAGRDRL AMNFERAAEL TAVPDDRILE
     IYNALRPYRS TKDELMAIAD DLENRYQAKI CAAFVREAAA LYVERKKLKG DD