PDUG_SALTY
ID PDUG_SALTY Reviewed; 610 AA.
AC O31043; Q7BV82;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Propanediol dehydratase-reactivating factor large subunit {ECO:0000250|UniProtKB:O68195};
DE Short=DDR large subunit;
DE AltName: Full=Propanediol utilization protein PduG;
GN Name=pduG {ECO:0000303|PubMed:10498708}; OrderedLocusNames=STM2043;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND INDUCTION.
RC STRAIN=LT2;
RX PubMed=10498708; DOI=10.1128/jb.181.19.5967-5975.1999;
RA Bobik T.A., Havemann G.D., Busch R.J., Williams D.S., Aldrich H.C.;
RT "The propanediol utilization (pdu) operon of Salmonella enterica serovar
RT typhimurium LT2 includes genes necessary for formation of polyhedral
RT organelles involved in coenzyme B(12)-dependent 1, 2-propanediol
RT degradation.";
RL J. Bacteriol. 181:5967-5975(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-7, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=12923081; DOI=10.1128/jb.185.17.5086-5095.2003;
RA Havemann G.D., Bobik T.A.;
RT "Protein content of polyhedral organelles involved in coenzyme B12-
RT dependent degradation of 1,2-propanediol in Salmonella enterica serovar
RT Typhimurium LT2.";
RL J. Bacteriol. 185:5086-5095(2003).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=9023178; DOI=10.1128/jb.179.4.1013-1022.1997;
RA Walter D., Ailion M., Roth J.;
RT "Genetic characterization of the pdu operon: use of 1,2-propanediol in
RT Salmonella typhimurium.";
RL J. Bacteriol. 179:1013-1022(1997).
RN [5]
RP SYSTEM-MODELING, AND FUNCTION.
RC STRAIN=LT2;
RX PubMed=28475631; DOI=10.1371/journal.pcbi.1005525;
RA Jakobson C.M., Tullman-Ercek D., Slininger M.F., Mangan N.M.;
RT "A systems-level model reveals that 1,2-Propanediol utilization
RT microcompartments enhance pathway flux through intermediate
RT sequestration.";
RL PLoS Comput. Biol. 13:e1005525-e1005525(2017).
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: 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:28475631}.
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:0000305|PubMed:10498708}.
CC -!- SUBUNIT: Forms a heterotetramer PduG(2)/PduH(2).
CC {ECO:0000250|UniProtKB:O68195}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:12923081}.
CC -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC medium. {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:9023178}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are defective in aerobic
CC degradation of propanediol. {ECO:0000269|PubMed:9023178}.
CC -!- MISCELLANEOUS: Bacterial microcompartments (BMC) 100-200 nm in cross
CC section are formed during aerobic growth on minimal 1,2-PD-B12 or
CC anaerobic growth on 1,2-PD-tetrathionate medium, but not during aerobic
CC growth on glucose, anerobic growth on glucose or pyruvate-tetrathionate
CC (PubMed:10498708). BMCs can constitute up to 10% of total cell protein
CC (PubMed:12923081). {ECO:0000269|PubMed:10498708,
CC ECO:0000269|PubMed:12923081}.
CC -!- SIMILARITY: Belongs to the DdrA/PduG family. {ECO:0000305}.
CC -!- CAUTION: Originally suggested to encode a cobalamin adenosyl
CC transferase. {ECO:0000305|PubMed:9023178}.
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DR EMBL; AF026270; AAB84105.2; -; Genomic_DNA.
DR EMBL; AE006468; AAL20947.1; -; Genomic_DNA.
DR RefSeq; NP_460988.1; NC_003197.2.
DR RefSeq; WP_001268876.1; NC_003197.2.
DR AlphaFoldDB; O31043; -.
DR STRING; 99287.STM2043; -.
DR PaxDb; O31043; -.
DR EnsemblBacteria; AAL20947; AAL20947; STM2043.
DR GeneID; 1253564; -.
DR KEGG; stm:STM2043; -.
DR PATRIC; fig|99287.12.peg.2165; -.
DR HOGENOM; CLU_449540_0_0_6; -.
DR OMA; LFHIRHE; -.
DR PhylomeDB; O31043; -.
DR BioCyc; SENT99287:STM2043-MON; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031472; C:propanediol degradation polyhedral organelle; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Bacterial microcompartment; Chaperone;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..610
FT /note="Propanediol dehydratase-reactivating factor large
FT subunit"
FT /id="PRO_0000454262"
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"
FT CONFLICT 7
FT /note="I -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000269|PubMed:12923081"
SQ SEQUENCE 610 AA; 64512 MW; 1146F7F56D183883 CRC64;
MRYIAGIDIG NSSTEVALAR QDETGALTIT HSALAETTGI KGTLRNVFGI QEALALVAKR
AGINVRDISL IRINEATPVI GDVAMETITE TIITESTMIG HNPKTPGGAG LGVGITITPE
ELLTRPADSS YILVVSSAFD FADIANVINA SMRAGYQITG VILQRDDGVL VSNRLEKSLP
IVDEVLYIDR IPLGMLAAIE VAVPGKVIET LSNPYGIATV FNLNADETKN IVPMARALIG
NRSAVVVKTP SGDVKARAIP AGNLELQAQG RTVRVDVAAG AEAIMKAVDG CGKLDNVTGE
AGTNIGGMLE HVRQTMAELT NKPSSEIFIQ DLLAVDTSVP VSVTGGLAGE FSLEQAVGIA
SMVKSDRLQM AMIAREIEQK LNIDVQIGGA EAEAAILGAL TTPGTTRPLA ILDLGAGSTD
ASIINPKGEI IATHLAGAGD MVTMIIAREL GLEDRYLAEE IKKYPLAKVE SLFHLRHEDG
SVQFFPTPLP PAVFARVCVV KPDELVPLPG DLALEKVRAI RRSAKERVFV TNALRALRQV
SPTGNIRDIP FVVLVGGSSL DFEVPQLVTD ALAHYRLVAG RGNIRGSEGP RNAVATGLIL
SWHKEFAHGQ
