ID MHPF_SHISS Reviewed; 316 AA. AC Q3Z555; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 30. DE RecName: Full=Acetaldehyde dehydrogenase; DE EC=1.2.1.10; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating]; GN Name=mhpF; OrderedLocusNames=SSON_0330; OS Shigella sonnei (strain Ss046). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=300269; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16275786; DOI=10.1093/nar/gki954; RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., RA Qiang B., Hou Y., Yu J., Jin Q.; RT "Genome dynamics and diversity of Shigella species, the etiologic RT agents of bacillary dysentery."; RL Nucleic Acids Res. 33:6445-6458(2005). CC -!- FUNCTION: Catalyzes the terminal reaction in meta-cleavage CC pathways, that is, the transformation of acetaldehyde into acetyl CC coenzyme A (By similarity). CC -!- CATALYTIC ACTIVITY: Acetaldehyde + CoA + NAD(+) = acetyl-CoA + CC NADH. CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid CC degradation. CC -!- SUBUNIT: Interacts with mhpE (By similarity). CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family. MhpF CC subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000038; AAZ87107.1; -; Genomic_DNA. DR RefSeq; YP_309342.1; -. DR SMR; Q3Z555; 3-308. DR GeneID; 3668929; -. DR GenomeReviews; CP000038_GR; SSON_0330. DR KEGG; ssn:SSON_0330; -. DR HOGENOM; Q3Z555; -. DR OMA; Q3Z555; HVKNDAF. DR BioCyc; SSON300269:SSO_0330-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) ac...; IEA:HAMAP. DR GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro. DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro. DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:HAMAP. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01657; -; 1. DR InterPro; IPR003361; Acetaldehyde_dehydrogenase. DR InterPro; IPR015426; Acetylaldehyde_DH_C. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR PANTHER; PTHR21123; Acetylald_dh; 1. DR Pfam; PF09290; AcetDehyd-dimer; 1. DR Pfam; PF01118; Semialdhyde_dh; 1. DR PIRSF; PIRSF015689; Actaldh_dh_actl; 1. DR TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1. PE 3: Inferred from homology; KW Aromatic hydrocarbons catabolism; Complete proteome; NAD; KW Oxidoreductase. FT CHAIN 1 316 Acetaldehyde dehydrogenase. FT /FTId=PRO_0000337985. SQ SEQUENCE 316 AA; 33442 MW; A6918BDA5EF4876B CRC64; MSKRKVAIIG SGNIGTDLMI KILRHGQHLE MAVMVGIDPQ SDGLARARRM GVATTHEGVI GLMNMPEFAD IDIVFDATSA GAHVKNDAAL REAKPDIRLI DLTPAAIGPY CVPVVNLEAN VDQLNVNMVT CGGQATIPMV AAVSRVARVH YAEIIASIAS KSAGPGTRAN IDEFTETTSR AIEVVGGAAK GKAIIVLNPA EPPLMMRDTV YVLSDEASQD DIEASINEMA EAVQAYVPGY RLKQRVQFEV IPQDKPVNLP GVGQFSGLKT AVWLEVEGAA HYLPAYAGNL DIMTSSALAT AEKMAQSLAR KAGEAA //