ID   ALDH_PARDP              Reviewed;         508 AA.
AC   A1B4L2;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000303|PubMed:23603744};
DE            EC=1.2.1.3 {ECO:0000269|PubMed:23603744};
DE   AltName: Full=Acetaldehyde dehydrogenase {ECO:0000305};
GN   Name=adh {ECO:0000303|PubMed:23603744};
GN   OrderedLocusNames=Pden_2366 {ECO:0000312|EMBL:ABL70456.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=Pd 1222;
RX   PubMed=23603744; DOI=10.1128/jb.00307-13;
RA   Felux A.K., Denger K., Weiss M., Cook A.M., Schleheck D.;
RT   "Paracoccus denitrificans PD1222 utilizes hypotaurine via transamination
RT   followed by spontaneous desulfination to yield acetaldehyde and, finally,
RT   acetate for growth.";
RL   J. Bacteriol. 195:2921-2930(2013).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of acetaldehyde to
CC       acetate. {ECO:0000269|PubMed:23603744}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000269|PubMed:23603744};
CC   -!- PATHWAY: Organosulfur degradation. {ECO:0000269|PubMed:23603744}.
CC   -!- INDUCTION: Induced by growth on hypotaurine.
CC       {ECO:0000269|PubMed:23603744}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000489; ABL70456.1; -; Genomic_DNA.
DR   RefSeq; WP_011748649.1; NC_008686.1.
DR   AlphaFoldDB; A1B4L2; -.
DR   SMR; A1B4L2; -.
DR   STRING; 318586.Pden_2366; -.
DR   PRIDE; A1B4L2; -.
DR   EnsemblBacteria; ABL70456; ABL70456; Pden_2366.
DR   KEGG; pde:Pden_2366; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_5; -.
DR   OMA; HGIGYYP; -.
DR   BioCyc; MetaCyc:MON-18239; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..508
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000446014"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
SQ   SEQUENCE   508 AA;  55725 MW;  00DB56CAB62E1BB9 CRC64;
     MPNDQTHPFR GVNALPFEER YDNFIGGEWV APVSGRYFTN TTPITGAEIG QIARSEAGDI
     ELALDAAHAA KEKWGATSPA ERANIMLKIA DRMERNLELL ATAETWDNGK PIRETMAADL
     PLAIDHFRYF AGVLRAQEGS ISQIDDDTVA YHFHEPLGVV GQIIPWNFPL LMACWKLAPA
     IAAGNCVVLK PAEQTPAGIM VWANLIGDLL PPGVLNIVNG FGLEAGKPLA SSNRIAKIAF
     TGETTTGRLI MQYASENLIP VTLELGGKSP NIFFADVARE DDDFFDKALE GFTMFALNQG
     EVCTCPSRVL IQESIYDKFM ERAVQRVQAI KQGDPRESDT MIGAQASSEQ KEKILSYLDI
     GKKEGAEVLT GGKAADLGGE LSGGYYIEPT IFRGNNKMRI FQEEIFGPVV SVTTFKDQAE
     ALEIANDTLY GLGAGVWSRD ANTCYRMGRG IKAGRVWTNC YHAYPAHAAF GGYKQSGIGR
     ETHKMMLDHY QQTKNMLVSY SPKKLGFF