PDUQ_SALTY
ID PDUQ_SALTY Reviewed; 370 AA.
AC Q9XDN0; Q7BV75;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=1-propanol dehydrogenase PduQ {ECO:0000303|PubMed:23077559};
DE EC=1.1.-.- {ECO:0000269|PubMed:23077559};
DE AltName: Full=Propanediol utilization protein PduQ;
GN Name=pduQ {ECO:0000303|PubMed:10498708}; OrderedLocusNames=STM2052;
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 1-9; 272-278 AND 337-351, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION
RP WITH PDUP, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=23077559; DOI=10.1371/journal.pone.0047144;
RA Cheng S., Fan C., Sinha S., Bobik T.A.;
RT "The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+
RT internally within the Pdu microcompartment of Salmonella enterica.";
RL PLoS ONE 7:e47144-e47144(2012).
RN [4]
RP BACTERIAL MICROCOMPARTMENT ABUNDANCE.
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 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: An iron-dependent alcohol dehydrogenase required for optimal
CC 1,2-propanediol (1,2-PD) degradation. NAD(+) and NADH are regenerated
CC internally within the bacterial microcompartment (BMC) dedicated to
CC 1,2-PD degradation by the PduP and PduQ enzymes, which reduce NAD(+)
CC and oxidize NADH respectively, although there must also be cofactor
CC transport across the BMC. {ECO:0000269|PubMed:23077559}.
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=1-propanol + NAD(+) = H(+) + NADH + propanal;
CC Xref=Rhea:RHEA:50704, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:28831, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:23077559};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50705;
CC Evidence={ECO:0000269|PubMed:23077559};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50706;
CC Evidence={ECO:0000269|PubMed:23077559};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:23077559};
CC -!- ACTIVITY REGULATION: Enzyme is oxygen sensitive.
CC {ECO:0000269|PubMed:23077559}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.3 uM for NADH {ECO:0000269|PubMed:23077559};
CC KM=16.0 mM for propanal {ECO:0000269|PubMed:23077559};
CC KM=267.5 uM for NAD(+) {ECO:0000269|PubMed:23077559};
CC KM=95.8 mM for 1-propanol {ECO:0000269|PubMed:23077559};
CC Vmax=77.7 umol/min/mg enzyme for propanal
CC {ECO:0000269|PubMed:23077559};
CC Vmax=9.2 umol/min/mg enzyme for 1-propanol
CC {ECO:0000269|PubMed:23077559};
CC pH dependence:
CC Optimum pH is 7.0 for propionaldehyde reduction and 9.0 for 1-
CC propanol dehydrogenase. {ECO:0000269|PubMed:23077559};
CC -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC {ECO:0000305|PubMed:10498708}.
CC -!- SUBUNIT: Interacts with PduP, probably via the N-terminus of PduQ.
CC {ECO:0000269|PubMed:23077559}.
CC -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC {ECO:0000269|PubMed:12923081}. Note=Probably located inside the BMC
CC shell. {ECO:0000305|PubMed:23077559}.
CC -!- INDUCTION: BMC production is induced by growth on 1,2-PD vitamin B12
CC medium. {ECO:0000269|PubMed:10498708}.
CC -!- DISRUPTION PHENOTYPE: Loss of NADH-dependent reduction of
CC propionaldehyde in BMCs. BMCs appear to be normal, cells grow more
CC slowly on 1,2-PD with limiting or saturating CN-B12.
CC {ECO:0000269|PubMed:12923081}.
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 iron-containing alcohol dehydrogenase
CC family. {ECO:0000305|PubMed:23077559}.
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DR EMBL; AF026270; AAD39016.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20956.1; -; Genomic_DNA.
DR RefSeq; NP_460997.1; NC_003197.2.
DR RefSeq; WP_001091448.1; NC_003197.2.
DR AlphaFoldDB; Q9XDN0; -.
DR STRING; 99287.STM2052; -.
DR PaxDb; Q9XDN0; -.
DR EnsemblBacteria; AAL20956; AAL20956; STM2052.
DR GeneID; 1253573; -.
DR KEGG; stm:STM2052; -.
DR PATRIC; fig|99287.12.peg.2174; -.
DR HOGENOM; CLU_007207_0_0_6; -.
DR OMA; GDCLATR; -.
DR PhylomeDB; Q9XDN0; -.
DR BioCyc; MetaCyc:STM2052-MON; -.
DR BioCyc; SENT99287:STM2052-MON; -.
DR UniPathway; UPA00621; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0031472; C:propanediol degradation polyhedral organelle; IDA:UniProtKB.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0051144; P:propanediol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Direct protein sequencing; Iron; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..370
FT /note="1-propanol dehydrogenase PduQ"
FT /id="PRO_0000454270"
SQ SEQUENCE 370 AA; 39470 MW; 90BFDC8FEB08B475 CRC64;
MNTFSLQTRL YSGQGSLAVL KRFTNKHIWI ICDGFLAHSP LLDTLRNALP ADNRISVFSE
ITPDPTIHTV VQGIAQMQAL QPQVVIGFGG GSAMDAAKAI VWFSQQSGIN IETCVAIPTT
SGTGSEVTSA CVISDPDKGI KYPLFNNALY PDMAILDPEL VVSVPPQITA NTGMDVLTHA
LEAWVSPRAS DFTDALAEKA AKLVFQYLPT AVEKGDCVAT RGKMHNASTL AGMAFSQAGL
GLNHAIAHQL GGQFHLPHGL ANALLLTTVI RFNAGVPRAA KRYARLAKAC GFCPAEANDI
AAINALIQQI ELLKQRCVLP SLAVALKEGR SDFSARIPAM VQAALADVTL RTNPRPANAE
AIRELLEELL
