PDUG_CITFR
ID PDUG_CITFR Reviewed; 610 AA.
AC B1VB67;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Propanediol dehydratase-reactivating factor large subunit {ECO:0000250|UniProtKB:O68195, ECO:0000303|PubMed:18332146};
DE Short=DDR large subunit;
DE AltName: Full=Propanediol utilization protein PduG;
GN Name=pduG {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: Large 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. This
CC subunit contains the adenosine nucleotide binding site.
CC {ECO:0000250|UniProtKB:O68195}.
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:O68195};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O68195};
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:O68195}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000250|UniProtKB:O31043}.
CC -!- SIMILARITY: Belongs to the DdrA/PduG family. {ECO:0000305}.
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DR EMBL; AM498294; CAM57288.1; -; Genomic_DNA.
DR RefSeq; WP_019077098.1; NZ_LIDR01000043.1.
DR UniPathway; UPA00621; -.
DR GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 2.40.50.140; -; 1.
DR Gene3D; 3.50.30.70; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR030994; DDR_dom.
DR InterPro; IPR040916; DDR_swiveling.
DR InterPro; IPR009191; DDRA.
DR InterPro; IPR028975; DDRA_swiveling_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF08841; DDR; 1.
DR Pfam; PF18427; DDR_swiveling; 1.
DR PIRSF; PIRSF011502; DdrA_PduG; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR SUPFAM; SSF82317; SSF82317; 1.
DR TIGRFAMs; TIGR04491; reactive_PduG; 1.
PE 3: Inferred from homology;
KW ATP-binding; Bacterial microcompartment; Chaperone; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide-binding.
FT CHAIN 1..610
FT /note="Propanediol dehydratase-reactivating factor large
FT subunit"
FT /id="PRO_0000454261"
FT BINDING 11..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O68195"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O68195"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O68195"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O68195"
FT BINDING 459..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O68195"
FT BINDING 557..558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O68195"
FT BINDING 591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O68195"
SQ SEQUENCE 610 AA; 64164 MW; 974641778B3EBE82 CRC64;
MRYIAGIDIG NSSTEVALAT LDESGALSIT GSALAETTGI KGTLRNVFGI QEALSLAAKN
AGINVSDISL IRINEATPVI GDVAMETITE TIITESTMIG HNPKTPGGVG LGVGVTITPE
DLLSRPADTP YILVVSSAFD FADVATMINA SVRAGYQLTG VILQQDDGVL VSNRLTHPLP
IVDEVLHIDR IPLGMLAAIE VAIPGKVIET LSNPYGIATV FGLNADETKN IVPMARALIG
NRSAVVVKTP SGDVKARAIP AGNLELQSQG RTVRVDVAAG AEAIMKAVGE CPKLDNVTGE
AGTNIGGMLE HVRQTMAELT NKPSHEIFIQ DLLAVDTSVP VSVTGGLAGE FSLEQAVGIA
SMVKSDRLQM AMIAQEITQK LNIDVQVGGA EAEAAILGAL TTPGTTRPLA ILDLGAGSTD
ASIINPKGEI IATHLAGAGD MVTMIIAREL GLEDRYLAEE IKKYPLAKVE SLFHLRHEDG
SVQFFPTPLP PTVFARVCVV KPDELVPLPG ELALEKVRAI RRSAKERVFV TNALRALRQV
SPTGNIRDIP FVVLVGGSSL DFEVPQLVTD ALAHYRLVAG RGNIRGTEGP RNAVATGLIL
SWYKAFAHGK
