ID   ADHE_BILW3              Reviewed;         484 AA.
AC   E5Y379;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Acetaldehyde dehydrogenase (acetylating) {ECO:0000305|PubMed:30718429};
DE            EC=1.2.1.10 {ECO:0000269|PubMed:30718429};
DE   AltName: Full=CoA-acylating acetaldehyde dehydrogenase {ECO:0000303|PubMed:30718429};
GN   Name=adhE {ECO:0000303|PubMed:30718429};
GN   ORFNames=HMPREF0179_00640 {ECO:0000312|EMBL:EFV45545.1};
OS   Bilophila wadsworthia (strain 3_1_6).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Bilophila.
OX   NCBI_TaxID=563192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_6;
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bilophila wadsworthia 3_1_6.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND PATHWAY.
RC   STRAIN=3_1_6;
RX   PubMed=30718429; DOI=10.1073/pnas.1815661116;
RA   Peck S.C., Denger K., Burrichter A., Irwin S.M., Balskus E.P.,
RA   Schleheck D.;
RT   "A glycyl radical enzyme enables hydrogen sulfide production by the human
RT   intestinal bacterium Bilophila wadsworthia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:3171-3176(2019).
CC   -!- FUNCTION: Involved in an anaerobic respiration pathway that converts
CC       the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and
CC       sulfide. Catalyzes the oxidation of acetaldehyde to acetyl-CoA in the
CC       presence of CoASH and NAD(+). Highly prefers NAD(+) over NADP(+).
CC       {ECO:0000269|PubMed:30718429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC         Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.10;
CC         Evidence={ECO:0000269|PubMed:30718429};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23289;
CC         Evidence={ECO:0000305|PubMed:30718429};
CC   -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC       {ECO:0000305|PubMed:30718429}.
CC   -!- INDUCTION: Highly up-regulated in the presence of taurine or
CC       isethionate. {ECO:0000269|PubMed:30718429}.
CC   -!- MISCELLANEOUS: Taurine is an abundant dietary and host-derived molecule
CC       whose metabolism to hydrogen sulfide (H2S) by members of the human gut
CC       microbiota has many prominent connections to host health and disease.
CC       The human gut bacterium and opportunistic pathogen Bilophila
CC       wadsworthia produces H2S when respiring sulfite (HSO3-) released from
CC       organosulfonate substrates such as taurine and isethionate.
CC       {ECO:0000305|PubMed:30718429}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; ADCP02000001; EFV45545.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5Y379; -.
DR   SMR; E5Y379; -.
DR   STRING; 563192.HMPREF0179_00640; -.
DR   EnsemblBacteria; EFV45545; EFV45545; HMPREF0179_00640.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_028794_1_0_7; -.
DR   BioCyc; MetaCyc:MON-20853; -.
DR   UniPathway; UPA00338; -.
DR   Proteomes; UP000006034; Unassembled WGS sequence.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07121; ALDH_EutE; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR012408; Acetald_propionald_DH-rel.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036410; EutE_PduP; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..484
FT                   /note="Acetaldehyde dehydrogenase (acetylating)"
FT                   /id="PRO_0000450949"
SQ   SEQUENCE   484 AA;  51386 MW;  8EE50C860BDDCA16 CRC64;
     MDVRQQDVER IVVEVLKKMM SDQPTAAATT VVAASGCDCG DFGLFDRLED AVQAAEAAQK
     KISTVAMRDK IIAAIRKAGL ENAKAFAEIA HNETGMGRVS DKIAKNILVC ERTPGTECLS
     PMAISGDMGL TLIENAPWGV IASVTPSTNP TATVINNAIS MIAGGNSVIF APHPNAKRAS
     QTAIQVLNKA IIEATGVANL LVAVKEPTIE VAQELFSHPR IKLLVVTGGE AVVAQARKVA
     TMRLIAAGAG NPPVVVDETA NIARAARSIY DGASFDNNII CADEKEIIAV DSIADQLKAE
     MKAIGAVEIS LEQADAVARV VLRNYPQVEG GKAPNPNPKW VGRDAALIAK AAGIDVPDSC
     RLLIVDVKRD INHVFARVEQ LMPVIPLLRA ANVDEAIEWA LILERGLSHT AGMHSRNIDN
     MDKMARAMNT SLFVKNGPHL AALGAGGEGW TTMTISTPTG EGVTCARSFV RLRRCCVVDN
     FRIV