ID   PDUH_CITFR              Reviewed;         116 AA.
AC   B1VB68;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Propanediol dehydratase-reactivating factor small subunit {ECO:0000250|UniProtKB:O68196, ECO:0000303|PubMed:18332146};
DE            Short=DDR small subunit;
DE   AltName: Full=Propanediol utilization protein PduH;
GN   Name=pduH {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, AND PATHWAY.
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: Small subunit of the propanediol dehydratase-reactivating
CC       factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-
CC       dependent propanediol dehydratase (diol dehydratase, DDH) found in the
CC       bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD)
CC       degradation. Reactivates inactivated DDH in the presence of ATP, Mg(2+)
CC       and free adenosylcobalamin (AdoCbl), by mediating the exchange of the
CC       tightly bound damaged cofactor AdoCbl for a free intact one.
CC       {ECO:0000250|UniProtKB:O68196}.
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=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O68196};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O68196};
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- SUBUNIT: Forms a heterotetramer PduG(2)/PduH(2).
CC       {ECO:0000250|UniProtKB:O68196}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000250|UniProtKB:Q8ZNR6}.
CC   -!- SIMILARITY: Belongs to the DdrB/PduH family. {ECO:0000305}.
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DR   EMBL; AM498294; CAM57289.1; -; Genomic_DNA.
DR   UniPathway; UPA00621; -.
DR   GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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; IPR009192; Diol/glycerol_deHydtase_re_ssu.
DR   Pfam; PF02288; Dehydratase_MU; 1.
DR   PIRSF; PIRSF011503; DdrB_PduH; 1.
DR   SUPFAM; SSF52968; SSF52968; 1.
PE   3: Inferred from homology;
KW   Bacterial microcompartment; Chaperone; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..116
FT                   /note="Propanediol dehydratase-reactivating factor small
FT                   subunit"
FT                   /id="PRO_0000454263"
FT   BINDING         31
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O68196"
SQ   SEQUENCE   116 AA;  12632 MW;  D25AD96D763E0758 CRC64;
     MESNLTTPAI VIFATAGCTD VWGDVLLGIE EEGIPFVIQE SPSTDVIHNA WLAACQSPLL
     VGIGCSREKL VVHYKNLPTS APLFTLTYQQ DNHARRSIGN NAARLVKGIP FRECHS