ID ABDH_SERP5 Reviewed; 474 AA. AC A8GHZ8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 04-NOV-2026, entry version 110. DE RecName: Full=Gamma-aminobutyraldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275}; DE Short=ABALDH {ECO:0000255|HAMAP-Rule:MF_01275}; DE EC=1.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01275}; DE AltName: Full=1-pyrroline dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275}; DE AltName: Full=4-aminobutanal dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275}; DE AltName: Full=5-aminopentanal dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01275}; DE EC=1.2.1.- {ECO:0000255|HAMAP-Rule:MF_01275}; GN Name=patD {ECO:0000255|HAMAP-Rule:MF_01275}; GN OrderedLocusNames=Spro_3642; OS Serratia proteamaculans (strain 568). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Yersiniaceae; Serratia. OX NCBI_TaxID=399741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=568; RX PubMed=19060168; DOI=10.1128/aem.02239-08; RA Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N., RA Barac T., Vangronsveld J., van der Lelie D.; RT "Genome survey and characterization of endophytic bacteria exhibiting a RT beneficial effect on growth and development of poplar trees."; RL Appl. Environ. Microbiol. 75:748-757(2009). CC -!- FUNCTION: Catalyzes the oxidation 4-aminobutanal (gamma- CC aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). CC This is the second step in one of two pathways for putrescine CC degradation, where putrescine is converted into 4-aminobutanoate via 4- CC aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a CC L-lysine degradation pathway to succinate that proceeds via cadaverine, CC glutarate and L-2-hydroxyglutarate. {ECO:0000255|HAMAP-Rule:MF_01275}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-aminobutanal + NAD(+) + H2O = 4-aminobutanoate + NADH + 2 CC H(+); Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264, CC ChEBI:CHEBI:59888; EC=1.2.1.19; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01275}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01275}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5-aminopentanal + NAD(+) + H2O = 5-aminopentanoate + NADH + 2 CC H(+); Xref=Rhea:RHEA:61632, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:144896, CC ChEBI:CHEBI:356010; Evidence={ECO:0000255|HAMAP-Rule:MF_01275}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61633; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01275}; CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4- CC aminobutanoate from 4-aminobutanal: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01275}. CC -!- PATHWAY: Amino-acid degradation. {ECO:0000255|HAMAP-Rule:MF_01275}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01275}. CC -!- MISCELLANEOUS: 4-aminobutanal can spontaneously cyclize to 1-pyrroline, CC and 5-aminopentanal to 1-piperideine. {ECO:0000255|HAMAP- CC Rule:MF_01275}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma- CC aminobutyraldehyde dehydrogenase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01275}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000826; ABV42738.1; -; Genomic_DNA. DR AlphaFoldDB; A8GHZ8; -. DR SMR; A8GHZ8; -. DR STRING; 399741.Spro_3642; -. DR PaxDb; 399741-Spro_3642; -. DR KEGG; spe:Spro_3642; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_0_0_6; -. DR OMA; AAFEHWG; -. DR OrthoDB; 9812625at2; -. DR UniPathway; UPA00188; UER00292. DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0019477; P:L-lysine catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniRule. DR CDD; cd07092; ALDH_ABALDH-YdcW; 1. DR FunFam; 3.40.605.10:FF:000001; Aldehyde dehydrogenase 1; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1. DR HAMAP; MF_01275; Aldedh_Prr; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR015657; Aminobutyraldehyde_DH. DR InterPro; IPR017749; PatD. DR NCBIfam; TIGR03374; ABALDH; 1. DR NCBIfam; NF010000; PRK13473.1; 1. DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW NAD; Oxidoreductase. FT CHAIN 1..474 FT /note="Gamma-aminobutyraldehyde dehydrogenase" FT /id="PRO_1000067395" FT ACT_SITE 246 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275" FT ACT_SITE 280 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275" FT BINDING 146..148 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275" FT BINDING 172..175 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275" FT BINDING 209 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275" FT BINDING 225..228 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275" FT BINDING 280 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01275" SQ SEQUENCE 474 AA; 50984 MW; E028C995EBC8A3FD CRC64; MQSQLLINGQ LVTGQGALLP VYNPATGEVV VQVAEASAEQ VDQAVLAADA AFEHWGQTTP KERAEHLLKL ADLIDSHAET FARLESINCG KPYHCVLNDE LPGVADVFRF FAGASRCLSG LAAGEYLAGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEQTPLT TFKLAELAAG LFPPGVLNVL FGRGASVGDR LTGHNKVRMV SLTGSIATGE HIIGHTASGI KRTHMELGGK APVLVFDDAD LQQVVEGIRS FGFYNAGQDC TAACRIYAQK GIYPQLVKAL GEAIGSLKIG PPIDASSELG PLITAQHLER VVGFVERAKA LPHVQVVTGG ERVNGPGYYF QPTLLAGARQ EDEIVQREVF GPVVTVTPFD DEAQVLAWAN ESDYGLASSL WTRDVGRAHR LSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSMYG LEDYTAIRHV MFKH //