ID   DHAT_CITFR              Reviewed;         387 AA.
AC   P45513;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=1,3-propanediol dehydrogenase {ECO:0000303|PubMed:7721705};
DE            EC=1.1.1.202 {ECO:0000269|PubMed:7721705};
DE   AltName: Full=1,3-propanediol oxidoreductase;
DE   AltName: Full=3-hydroxypropionaldehyde reductase;
GN   Name=dhaT {ECO:0000303|PubMed:7721705};
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], PROTEIN SEQUENCE OF 2-39, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK;
RX   PubMed=7721705; DOI=10.1128/jb.177.8.2151-2156.1995;
RA   Daniel R., Boenigk R., Gottschalk G.;
RT   "Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii
RT   and cloning, sequencing, and overexpression of the corresponding gene in
RT   Escherichia coli.";
RL   J. Bacteriol. 177:2151-2156(1995).
CC   -!- FUNCTION: Catalyzes the reduction of 3-hydroxypropanal. Is considerably
CC       less active with glyceraldehyde, propionaldehyde, acetaldehyde, and
CC       butyraldehyde. Also catalyzes the oxidation of various primary,
CC       secondary, and tertiary alcohols. Is most active with substrates
CC       containing two primary alcohol groups separated by one or two carbon
CC       atoms. 1,3-propanediol is the preferred substrate.
CC       {ECO:0000269|PubMed:7721705}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + propane-1,3-diol = 3-hydroxypropanal + H(+) + NADH;
CC         Xref=Rhea:RHEA:23188, ChEBI:CHEBI:15378, ChEBI:CHEBI:16109,
CC         ChEBI:CHEBI:17871, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.202; Evidence={ECO:0000269|PubMed:7721705};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23190;
CC         Evidence={ECO:0000269|PubMed:7721705};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000269|PubMed:7721705};
CC   -!- ACTIVITY REGULATION: Inhibited by the metal chelator 1,10-
CC       phenanthroline. {ECO:0000269|PubMed:7721705}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.14 mM for 3-hydroxypropanal {ECO:0000269|PubMed:7721705};
CC         KM=1.25 mM for 1,3-propanediol {ECO:0000269|PubMed:7721705};
CC         KM=11 mM for propionaldehyde {ECO:0000269|PubMed:7721705};
CC         KM=0.3 mM for NAD(+) (with 1,3-propanediol as substrate)
CC         {ECO:0000269|PubMed:7721705};
CC         KM=0.033 mM for NADH (with propionaldehyde as substrate)
CC         {ECO:0000269|PubMed:7721705};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:7721705}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; U09771; AAB48848.1; -; Genomic_DNA.
DR   PIR; A56275; A56275.
DR   RefSeq; WP_016157511.1; NZ_CABHHG010000021.1.
DR   AlphaFoldDB; P45513; -.
DR   SMR; P45513; -.
DR   STRING; 1333848.CFNIH1_02620; -.
DR   GeneID; 66272814; -.
DR   BRENDA; 1.1.1.202; 1398.
DR   GO; GO:0047516; F:1,3-propanediol dehydrogenase activity; IDA:CACAO.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..387
FT                   /note="1,3-propanediol dehydrogenase"
FT                   /id="PRO_0000087841"
SQ   SEQUENCE   387 AA;  41482 MW;  268F295DA83A8DCC CRC64;
     MSYRMFDYLV PNVNFFGPNA ISVVGERCKL LGGKKALLVT DKGLRAIKDG AVDKTLTHLR
     EAGIDVVVFD GVEPNPKDTN VRDGLEVFRK EHCDIIVTVG GGSPHDCGKG IGIAATHEGD
     LYSYAGIETL TNPLPPIVAV NTTAGTASEV TRHCVLTNTK TKVKFVIVSW RNLPSVSIND
     PLLMLGKPAP LTAATGMDAL THAVEAYISK DANPVTDAAA IQAIRLIARN LRQAVALGSN
     LKARENMAYA SLLAGMAFNN ANLGYVHAMA HQLGGLYDMP HGVANAVLLP HVARYNLIAN
     PEKFADIAEF MGENTDGLST MDAAELAIHA IARLSADIGI PQHLRDLGVK EADFPYMAEM
     ALKDGNAFSN PRKGNEKEIA EIFRQAF