位置:首页 > 蛋白库 > PDUE_SALTY
PDUE_SALTY
ID   PDUE_SALTY              Reviewed;         173 AA.
AC   O31042; Q7BV83;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Propanediol dehydratase small subunit;
DE            EC=4.2.1.28 {ECO:0000269|PubMed:25713376};
DE   AltName: Full=Diol dehydratase small subunit;
DE            Short=DDH small subunit;
DE   AltName: Full=Propanediol utilization protein PduE;
GN   Name=pduE {ECO:0000303|PubMed:9352910}; OrderedLocusNames=STM2042;
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   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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 2-ASN--SER-35.
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   [10]
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   [11]
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. Localized in the
CC       bacterial microcompartment (BMC) dedicated to 1,2-PD degradation.
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       Note=Probably located inside the BMC shell.
CC       {ECO:0000269|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       {ECO:0000269|PubMed:10498708, ECO:0000269|PubMed:1312999}.
CC   -!- DISRUPTION PHENOTYPE: A triple pduC-pduD-pduE deletion releases no
CC       acetaldehyde when grown on propanediol. {ECO:0000269|PubMed:16585748}.
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 small subunit
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF026270; AAB84104.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20946.1; -; Genomic_DNA.
DR   RefSeq; NP_460987.1; NC_003197.2.
DR   RefSeq; WP_001090597.1; NC_003197.2.
DR   AlphaFoldDB; O31042; -.
DR   SMR; O31042; -.
DR   STRING; 99287.STM2042; -.
DR   PaxDb; O31042; -.
DR   EnsemblBacteria; AAL20946; AAL20946; STM2042.
DR   GeneID; 1253563; -.
DR   KEGG; stm:STM2042; -.
DR   PATRIC; fig|99287.12.peg.2164; -.
DR   HOGENOM; CLU_120853_0_0_6; -.
DR   OMA; CAAWFEE; -.
DR   PhylomeDB; O31042; -.
DR   BioCyc; MetaCyc:STM2042-MON; -.
DR   BioCyc; SENT99287:STM2042-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   Gene3D; 1.10.1510.20; -; 1.
DR   InterPro; IPR003207; Ppandiol/glycerol_DeHydtase_su.
DR   InterPro; IPR036091; Prodiol/glycerol_DeHase__sf_su.
DR   Pfam; PF02287; Dehydratase_SU; 1.
DR   PIRSF; PIRSF018505; Prpndl_dhdrts_sm; 1.
DR   SUPFAM; SSF47148; SSF47148; 1.
PE   1: Evidence at protein level;
KW   Bacterial microcompartment; Cobalamin; Cobalt; Direct protein sequencing;
KW   Lyase; Reference proteome.
FT   CHAIN           1..173
FT                   /note="Propanediol dehydratase small subunit"
FT                   /id="PRO_0000391460"
FT   MUTAGEN         2..35
FT                   /note="Missing: Enzyme associates with BMCs, 25% decrease
FT                   in enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:21821773"
SQ   SEQUENCE   173 AA;  19144 MW;  4E0012588EFB3916 CRC64;
     MNTDAIESMV RDVLSRMNSL QGDAPAAAPA AGGTSRSAKV SDYPLANKHP EWVKTATNKT
     LDDFTLENVL SNKVTAQDMR ITPETLRLQA SIAKDAGRDR LAMNFERAAE LTAVPDDRIL
     EIYNALRPYR STKEELLAIA DDLENRYQAK ICAAFVREAA GLYVERKKLK GDD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024