ID CALB_PSEUH Reviewed; 481 AA. AC O86447; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 39. DE RecName: Full=Coniferyl aldehyde dehydrogenase; DE Short=CALDH; DE EC=1.2.1.68; GN Name=calB; OS Pseudomonas sp. (strain HR199 / DSM 7063). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=86003; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, AND RP CHARACTERIZATION. RX MEDLINE=98389649; PubMed=9721273; RA Achterholt S., Priefert H., Steinbuechel A.; RT "Purification and characterization of the coniferyl aldehyde RT dehydrogenase from Pseudomonas sp. strain HR199 and molecular RT characterization of the gene."; RL J. Bacteriol. 180:4387-4391(1998). CC -!- FUNCTION: Catalyzes the NAD+-dependent oxidation of coniferyl CC aldehyde to ferulic acid and which is induced during growth with CC eugenol as the carbon source. CC -!- CATALYTIC ACTIVITY: Coniferyl aldehyde + H(2)O + NAD(P)(+) = CC ferulate + NAD(P)H. CC -!- SUBUNIT: Homodimer. CC -!- MISCELLANEOUS: The enzyme activity with NADP(+) is 4.3% of that CC with NAD(+). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. 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; AJ006231; CAA06926.1; -; Genomic_DNA. DR HSSP; P11883; 1AD3. DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro. DR GO; GO:0050269; F:coniferyl-aldehyde dehydrogenase activity; IEA:EC. DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR InterPro; IPR012394; Aldehyde_DH_NAD(P). DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR PANTHER; PTHR11699:SF15; ALDH; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF036492; ALDH; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; NAD; Oxidoreductase. FT INIT_MET 1 1 Removed. FT CHAIN 2 481 Coniferyl aldehyde dehydrogenase. FT /FTId=PRO_0000056585. FT ACT_SITE 221 221 By similarity. FT ACT_SITE 255 255 By similarity. SQ SEQUENCE 481 AA; 51987 MW; A1AC6CC1CB1D55B1 CRC64; MSILGLNGAP VGAEQLGSAL DRMKKAHLEQ GPANLELRLS RLDRAIAMLL ENREAIADAV SADFGNRSRE QTLLCDIAGS VASLKDSREH VAKWMEPEHH KAMFPGAEAR VEFQPLGVVG VISPWNFPIV LAFGPLAGIF AAGNRAMLKP SELTPRTSAL LAELIARYFD ETELTTVLGD AEVGALFSAQ PFDHLIFTGG TAVAKHIMRA AADNLVPVTL ELGGKSPVIV SRSADMADVA QRVLTVKTFN AGQICLAPDY VLLPEESLDS FVAEATRFVA AMYPSLLDNP DYTSIINARN FDRLHRYLTD AQAKGGRVIE INPAAEELGD SGIRKIAPTL IVNVSDEMLV LNEEIFGPLL PIKTYRDFDS AIDYVNSKQR PLASYFFGED AVEREQVLKR TVSGAVVVND VMSHVMMDTL PFGGVGHSGM GAYHGIYGFR TFSHAKPVLV QSPVGESNLA MRAPYGEAIH GLLSVLLSTE C //