PDUC_SALTY
ID PDUC_SALTY Reviewed; 554 AA.
AC P37450;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Propanediol dehydratase large subunit;
DE EC=4.2.1.28 {ECO:0000269|PubMed:9352910};
DE AltName: Full=Diol dehydratase large subunit;
DE Short=DDH large subunit;
DE AltName: Full=Propanediol utilization protein PduC;
GN Name=pduC {ECO:0000303|PubMed:9352910}; OrderedLocusNames=STM2040;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC STRAIN=LT2;
RX PubMed=9352910; DOI=10.1128/jb.179.21.6633-6639.1997;
RA Bobik T.A., Xu Y., Jeter R.M., Otto K.E., Roth J.R.;
RT "Propanediol utilization genes (pdu) of Salmonella typhimurium: three genes
RT for the propanediol dehydratase.";
RL J. Bacteriol. 179:6633-6639(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, SUBCELLULAR LOCATION, AND
RP 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC STRAIN=LT2;
RX PubMed=8071226; DOI=10.1128/jb.176.17.5474-5482.1994;
RA Chen P., Anderson D.I., Roth J.R.;
RT "The control region of the pdu/cob regulon in Salmonella typhimurium.";
RL J. Bacteriol. 176:5474-5482(1994).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=11844753; DOI=10.1128/jb.184.5.1253-1261.2002;
RA Havemann G.D., Sampson E.M., Bobik T.A.;
RT "PduA is a shell protein of polyhedral organelles involved in coenzyme
RT B(12)-dependent degradation of 1,2-propanediol in Salmonella enterica
RT serovar typhimurium LT2.";
RL J. Bacteriol. 184:1253-1261(2002).
RN [7]
RP COFACTOR.
RX PubMed=2166132; DOI=10.1099/00221287-136-5-887;
RA Jeter R.M.;
RT "Cobalamin-dependent 1,2-propanediol utilization by Salmonella
RT typhimurium.";
RL J. Gen. Microbiol. 136:887-896(1990).
RN [8]
RP INDUCTION.
RX PubMed=1312999; DOI=10.1128/jb.174.7.2253-2266.1992;
RA Bobik T.A., Ailion M., Roth J.R.;
RT "A single regulatory gene integrates control of vitamin B12 synthesis and
RT propanediol degradation.";
RL J. Bacteriol. 174:2253-2266(1992).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN PROPANEDIOL UTILIZATION.
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 [10]
RP DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=16585748; DOI=10.1128/jb.188.8.2865-2874.2006;
RA Penrod J.T., Roth J.R.;
RT "Conserving a volatile metabolite: a role for carboxysome-like organelles
RT in Salmonella enterica.";
RL J. Bacteriol. 188:2865-2874(2006).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=21821773; DOI=10.1128/jb.05661-11;
RA Fan C., Bobik T.A.;
RT "The N-terminal region of the medium subunit (PduD) packages
RT adenosylcobalamin-dependent diol dehydratase (PduCDE) into the Pdu
RT microcompartment.";
RL J. Bacteriol. 193:5623-5628(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=27063436; DOI=10.1038/srep24359;
RA Held M., Kolb A., Perdue S., Hsu S.Y., Bloch S.E., Quin M.B.,
RA Schmidt-Dannert C.;
RT "Engineering formation of multiple recombinant Eut protein nanocompartments
RT in E. coli.";
RL Sci. Rep. 6:24359-24359(2016).
RN [13]
RP ACTIVITY REGULATION.
RC STRAIN=LT2;
RX PubMed=25713376; DOI=10.1073/pnas.1423672112;
RA Chowdhury C., Chun S., Pang A., Sawaya M.R., Sinha S., Yeates T.O.,
RA Bobik T.A.;
RT "Selective molecular transport through the protein shell of a bacterial
RT microcompartment organelle.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:2990-2995(2015).
RN [14]
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: Part of the PduCDE complex that catalyzes the dehydration of
CC 1,2-propanediol (1,2-PD) to propionaldehyde. Required for S.typhimurium
CC growth on 1,2-PD as the sole carbon and energy source (Probable)
CC (PubMed:9023178). This subunit is directly targeted to the BMC (By
CC similarity). {ECO:0000250|UniProtKB:P0DUM7, ECO:0000269|PubMed:9023178,
CC ECO:0000305|PubMed:9352910}.
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:0000269|PubMed:25713376, ECO:0000305|PubMed:28475631}.
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:0000269|PubMed:9352910};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000269|PubMed:2166132};
CC -!- ACTIVITY REGULATION: Inhibited by glycerol.
CC {ECO:0000269|PubMed:25713376}.
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000305|PubMed:10498708}.
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:0000269|PubMed:9352910}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:11844753,
CC ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:21821773,
CC ECO:0000269|PubMed:27063436}. Note=Probably located inside the BMC
CC shell. {ECO:0000305|PubMed:10498708}.
CC -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC medium (PubMed:10498708). By either propanediol or glycerol
CC (PubMed:1312999). {ECO:0000269|PubMed:10498708,
CC ECO:0000269|PubMed:1312999}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are defective in aerobic
CC degradation of propanediol and display no propanediol dehydratase
CC activity (PubMed:9023178). A triple pduC-pduD-pduE deletion releases no
CC acetaldehyde when grown on propanediol (PubMed:16585748).
CC {ECO:0000269|PubMed:16585748, 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 diol/glycerol dehydratase large subunit
CC family. {ECO:0000305}.
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DR EMBL; AF026270; AAB84102.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20944.1; -; Genomic_DNA.
DR RefSeq; NP_460985.1; NC_003197.2.
DR RefSeq; WP_001256896.1; NC_003197.2.
DR AlphaFoldDB; P37450; -.
DR SMR; P37450; -.
DR STRING; 99287.STM2040; -.
DR PaxDb; P37450; -.
DR EnsemblBacteria; AAL20944; AAL20944; STM2040.
DR GeneID; 1253561; -.
DR KEGG; stm:STM2040; -.
DR PATRIC; fig|99287.12.peg.2162; -.
DR HOGENOM; CLU_022314_1_0_6; -.
DR OMA; KTPSNQC; -.
DR PhylomeDB; P37450; -.
DR BioCyc; MetaCyc:STM2040-MON; -.
DR BioCyc; SENT99287:STM2040-MON; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031472; C:propanediol degradation polyhedral organelle; IDA:UniProtKB.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050215; F:propanediol dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03687; Dehydratase_LU; 1.
DR Gene3D; 3.20.20.350; -; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR036999; Diol/glycerol_deHase_lsu_sf.
DR InterPro; IPR003206; Diol/glycerol_deHydtase_lsu.
DR Pfam; PF02286; Dehydratase_LU; 1.
DR PIRSF; PIRSF018507; Prpndl_dhdrts_lg; 1.
DR SUPFAM; SSF51703; SSF51703; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Cobalamin; Cobalt; Direct protein sequencing;
KW Lyase; Reference proteome.
FT CHAIN 1..554
FT /note="Propanediol dehydratase large subunit"
FT /id="PRO_0000079885"
FT CONFLICT 302
FT /note="C -> S (in Ref. 1; AAB84102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 60362 MW; 4A9DE6729C7942DA CRC64;
MRSKRFEALA KRPVNQDGFV KEWIEEGFIA MESPNDPKPS IKIVNGAVTE LDGKPVSEFD
LIDHFIARYG INLNRAEEVM AMDSVKLANM LCDPNVKRSE IVPLTTAMTP AKIVEVVSHM
NVVEMMMAMQ KMRARRTPSQ QAHVTNVKDN PVQIAADAAE GAWRGFDEQE TTVAVARYAP
FNAIALLVGS QVGRPGVLTQ CSLEEATELK LGMLGHTCYA ETISVYGTEP VFTDGDDTPW
SKGFLASSYA SRGLKMRFTS GSGSEVQMGY AEGKSMLYLE ARCIYITKAA GVQGLQNGSV
SCIGVPSAVP SGIRAVLAEN LICSSLDLEC ASSNDQTFTH SDMRRTARLL MQFLPGTDFI
SSGYSAVPNY DNMFAGSNED AEDFDDYNVI QRDLKVDGGL RPVREEDVIA IRNKAARALQ
AVFAGMGLPP ITDEEVEAAT YAHGSKDMPE RNIVEDIKFA QEIINKNRNG LEVVKALAQG
GFTDVAQDML NIQKAKLTGD YLHTSAIIVG DGQVLSAVND VNDYAGPATG YRLQGERWEE
IKNIPGALDP NEID
