ID   PDUQ_CITFR              Reviewed;         370 AA.
AC   B1VB76;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=1-propanol dehydrogenase PduQ {ECO:0000303|PubMed:18332146};
DE            EC=1.1.-.- {ECO:0000250|UniProtKB:Q9XDN0};
DE   AltName: Full=Propanediol utilization protein PduQ;
GN   Name=pduQ {ECO:0000303|PubMed:18332146};
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX   PubMed=18332146; DOI=10.1074/jbc.m709214200;
RA   Parsons J.B., Dinesh S.D., Deery E., Leech H.K., Brindley A.A., Heldt D.,
RA   Frank S., Smales C.M., Lunsdorf H., Rambach A., Gass M.H., Bleloch A.,
RA   McClean K.J., Munro A.W., Rigby S.E.J., Warren M.J., Prentice M.B.;
RT   "Biochemical and Structural Insights into Bacterial Organelle Form and
RT   Biogenesis.";
RL   J. Biol. Chem. 283:14366-14375(2008).
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:0000250|UniProtKB:Q9XDN0}.
CC   -!- FUNCTION: Expression of a cosmid containing the full 21-gene pdu operon
CC       in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the
CC       appearance of bacterial microcompartments (BMC) in its cytoplasm.
CC       {ECO:0000269|PubMed:18332146}.
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:18332146}.
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:0000250|UniProtKB:Q9XDN0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50705;
CC         Evidence={ECO:0000250|UniProtKB:Q9XDN0};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50706;
CC         Evidence={ECO:0000250|UniProtKB:Q9XDN0};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q9XDN0};
CC   -!- PATHWAY: Polyol metabolism; 1,2-propanediol degradation.
CC       {ECO:0000269|PubMed:18332146}.
CC   -!- SUBUNIT: Interacts with PduP, probably via the N-terminus of PduQ.
CC       {ECO:0000250|UniProtKB:Q9XDN0}.
CC   -!- SUBCELLULAR LOCATION: Bacterial microcompartment
CC       {ECO:0000250|UniProtKB:Q9XDN0}. Note=Probably located inside the BMC
CC       shell. {ECO:0000250|UniProtKB:Q9XDN0}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AM498294; CAM57297.1; -; Genomic_DNA.
DR   UniPathway; UPA00621; -.
DR   GO; GO:0031469; C:bacterial microcompartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
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   3: Inferred from homology;
KW   Bacterial microcompartment; Iron; NAD; Oxidoreductase.
FT   CHAIN           1..370
FT                   /note="1-propanol dehydrogenase PduQ"
FT                   /id="PRO_0000454269"
SQ   SEQUENCE   370 AA;  39703 MW;  D92CA7DAAE82F0EF CRC64;
     MKSFSLQTRL YSGQGSLDVL KRLTNKHIWI ICDGFLARSP LIEKLRDALP ADNHISIFSD
     ITPDPTINTV VQGIAQMQSL RPDVVIGFGG GSALDAAKAI VWFSRQFGIE IETCVAIPTT
     SGTGSEVTSA CVISDPDKGI KYPLFNNALY PDMAILDPTL VVSVPPAITA NTGMDVLTHA
     LEAYVSTKAS DFTDALAEKA AQIVFQYLPV AVSKGDCLAT RGKMHNASTL AGMAFSQAGL
     GINHAIAHQL GGQFHLPHGL ANALLLTHVI HFNARDPRAA KRYARFAKAC HLCPDNANDT
     AALNALIRHI ELLKKQCALP SFADALKDGK QAWSQRIPSM VQAALADVTL QTNPRVADAS
     AMQELLEELL