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LOCUS WP_001163872 474 aa linear BCT 03-JUN-2024 ACCESSION WP_001163872 VERSION WP_001163872.1 KEYWORDS RefSeq. SOURCE Escherichia ORGANISM Escherichia Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 474) AUTHORS Schneider,B.L. and Reitzer,L. TITLE Pathway and enzyme redundancy in putrescine catabolism in Escherichia coli JOURNAL J Bacteriol 194 (15), 4080-4088 (2012) PUBMED 22636776 REFERENCE 2 (residues 1 to 474) AUTHORS Samsonova,N.N., Smirnov,S.V., Novikova,A.E. and Ptitsyn,L.R. TITLE Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase JOURNAL FEBS Lett 579 (19), 4107-4112 (2005) PUBMED 16023116 REFERENCE 3 (residues 1 to 474) AUTHORS Gruez,A., Roig-Zamboni,V., Grisel,S., Salomoni,A., Valencia,C., Campanacci,V., Tegoni,M. and Cambillau,C. TITLE Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase JOURNAL J Mol Biol 343 (1), 29-41 (2004) PUBMED 15381418 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR03374.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..474 /organism="Escherichia" /db_xref="taxon:561" gene 1..474 /gene="patD" Protein 1..474 /product="aminobutyraldehyde dehydrogenase" /EC_number="1.2.1.19" /GO_function="GO:0019145 - aminobutyraldehyde dehydrogenase activity [Evidence IEA]" /GO_function="GO:0051287 - NAD binding [Evidence IEA]" /GO_process="GO:0009447 - putrescine catabolic process [Evidence IEA]" /calculated_mol_wt=50699 Region 2..473 /region_name="ABALDH" /note="1-pyrroline dehydrogenase; TIGR03374" /db_xref="CDD:132417" Site order(59,106,116,120..123,125..126,128,134..135,218,230, 233,240,247,412..416,419..420,422,425,427..432,441..443, 448..449,454,467..472) /site_type="other" /note="tetrameric interface [polypeptide binding]" /db_xref="CDD:143411" Site order(145..146,148,172,174..175,204,209,223..225,228,231, 246,248,280,327,378) /site_type="other" /note="NAD binding site [chemical binding]" /db_xref="CDD:143411" Site order(149,246,277,280) /site_type="active" /note="catalytic residues [active]" /db_xref="CDD:143411" Site order(279,438) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:143411" ORIGIN 1 mqhkllinge lvsgegekqp vynpatgdvl leiaeasaeq vdaavraada afaewgqttp 61 kvraecllkl advieengqv faelesrncg kplhsafnde ipaivdvfrf fagaarclng 121 laageylegh tsmirrdplg vvasiapwny plmmaawkla palaagncvv lkpseitplt 181 alklaelakd ifpagvinil fgrgktvgdp ltghpkvrmv sltgsiatge hiishtassi 241 krthmelggk apvivfddad ieavvegvrt fgyynagqdc taacriyaqk giydtlvekl 301 gaavatlksg apddestelg plsslahler vgkaveeaka tghikvitgg ekrkgngyyy 361 aptllagalq ddaivqkevf gpvvsvtpfd neeqvvnwan dsqyglassv wtkdvgrahr 421 vsarlqygct wvnthfmlvs emphggqkls gygkdmslyg ledytvvrhv mvkh