PDUH_SALTY
ID PDUH_SALTY Reviewed; 116 AA.
AC Q8ZNR6; Q9XDN8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Propanediol dehydratase-reactivating factor small subunit {ECO:0000250|UniProtKB:O68196};
DE Short=DDR small subunit;
DE AltName: Full=Propanediol utilization protein PduH;
GN Name=pduH {ECO:0000303|PubMed:10498708}; OrderedLocusNames=STM2044;
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 IDENTIFICATION BY MASS SPECTROMETRY, 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 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: 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: 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: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:0000305|PubMed:10498708}.
CC -!- SUBUNIT: Forms a heterotetramer PduG(2)/PduH(2).
CC {ECO:0000250|UniProtKB:O68196}.
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}.
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 DdrB/PduH family. {ECO:0000305}.
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DR EMBL; AF026270; AAD39008.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20948.1; -; Genomic_DNA.
DR RefSeq; NP_460989.1; NC_003197.2.
DR RefSeq; WP_000377961.1; NC_003197.2.
DR AlphaFoldDB; Q8ZNR6; -.
DR STRING; 99287.STM2044; -.
DR PaxDb; Q8ZNR6; -.
DR EnsemblBacteria; AAL20948; AAL20948; STM2044.
DR GeneID; 1253565; -.
DR KEGG; stm:STM2044; -.
DR PATRIC; fig|99287.12.peg.2166; -.
DR HOGENOM; CLU_139758_2_0_6; -.
DR OMA; AHRNTGN; -.
DR PhylomeDB; Q8ZNR6; -.
DR BioCyc; SENT99287:STM2044-MON; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031472; C:propanediol degradation polyhedral organelle; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Bacterial microcompartment; Chaperone; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..116
FT /note="Propanediol dehydratase-reactivating factor small
FT subunit"
FT /id="PRO_0000454264"
FT BINDING 31
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O68196"
FT CONFLICT 112..116
FT /note="RDLHA -> GISMLNHRRTAV (in Ref. 1; AAD39008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12656 MW; 731740F2BCDA336F CRC64;
MDSNHSAPAI VITVINDCAS LWHEVLLGIE EEGIPFLLQH HPAGDIVDSA WQAARSSPLL
VGIACDRHSL VVHYKNLPAS APLFTLMHHQ DSQAQRNTGN NAARLVKGIP FRDLHA
