ID MHPF_BURXL Reviewed; 313 AA. AC Q13QH7; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 25-NOV-2008, entry version 22. DE RecName: Full=Acetaldehyde dehydrogenase; DE EC=1.2.1.10; DE AltName: Full=Acetaldehyde dehydrogenase [acetylating]; GN Name=mhpF; OrderedLocusNames=Bxeno_B0694; ORFNames=Bxe_B2326; OS Burkholderia xenovorans (strain LB400). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., RA Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., RA Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M., RA Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., RA Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp RT genome shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). 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 -!- 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; CP000271; ABE33662.1; -; Genomic_DNA. DR RefSeq; YP_553012.1; -. DR SMR; Q13QH7; 3-313. DR GeneID; 4007178; -. DR GenomeReviews; CP000271_GR; Bxeno_B0694. DR KEGG; bxe:Bxe_B2326; -. DR HOGENOM; Q13QH7; -. DR BioCyc; BXEN266265:BXE_B2326-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 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; Acetylald_dehydrogenase. DR InterPro; IPR015426; Acetylald_DHase_C. DR InterPro; IPR000534; Semialdehyde_DHase_NAD-bd. DR InterPro; IPR006035; Ureohydrolase. 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 1 313 Acetaldehyde dehydrogenase. FT /FTId=PRO_0000337977. SQ SEQUENCE 313 AA; 32763 MW; F0A85325E5E6BAD5 CRC64; MASEKLKAAI IGSGNIGTDL MIKIMRHSEH LEMAAMVGID AASDGLARAA RLGVATTHEG VEGLTRLPVF DDIDFVFDAT SAGAHVKNDA FLRALKPGIR LIDLTPAAIG PYCVPVVNLD AHLDSRNVNM VTCGGQATIP MVAAVSRVAK VHYAEIVASI SSKSAGPGTR ANIDEFTETT SKAIEAVGGA AKGKAIIVLN PAEPPVMMRD TVYVLSDLAD RAQVEASIEA MAAAVHAYVP GYRLKQKVQF DEIAADVPLN IPGLGRFSGL KTSVFIEVEG AAHYLPAYAG NLDIMTSAAL ATAERMAQSL VQA //