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ABDH_SALCH
ID   ABDH_SALCH              Reviewed;         474 AA.
AC   Q57P61;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 102.
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}; OrderedLocusNames=SCH_1594;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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 + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC         NADH; 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 + H2O + NAD(+) = 5-aminopentanoate + 2 H(+) +
CC         NADH; 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   -!- SEQUENCE CAUTION:
CC       Sequence=AAX65500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017220; AAX65500.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q57P61; -.
DR   SMR; Q57P61; -.
DR   EnsemblBacteria; AAX65500; AAX65500; SCH_1594.
DR   KEGG; sec:SCH_1594; -.
DR   HOGENOM; CLU_005391_0_0_6; -.
DR   UniPathway; UPA00188; UER00292.
DR   Proteomes; UP000000538; Chromosome.
DR   GO; GO:0033737; F:1-pyrroline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019145; F:aminobutyraldehyde dehydrogenase 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   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR03374; ABALDH; 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_0000269697"
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;  51093 MW;  25CDAF63AD1CFB9C CRC64;
     MQYQLLINGV LVDGEGERQS VYNPATGEVI LEIAEASPAQ VDAAVLAADS AFAEWGQTTP
     KARAECLLKL ADSIEQNALE FARLESQNCG KPLHCVINDE IPAIVDVFRF FAGAARCLSG
     LAAGEYLEGH TSMIRRDPIG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT
     ALKLAALAKD IFPPGVLNVL FGRGQTVGDV LTGHEKVRMV SLTGSIATGE HILRHTAPAI
     KRTHMELGGK APVIVFDDAD LDAAAQGVRT FGFYNAGQDC TAACRIYAQR GIYDALVEKL
     GNAVSSLKMG APEDESTELG PLSSLAHLKR VTAAVEEAKA LSHIRVITGG SQTEGKGYYF
     APTLLADAKQ EDAIVQREVF GPVVSITVFD DEDQVLRWAN DSRYGLASSV WTQDVGRAHR
     LSARLQYGCT WINTHFMLVS EMPHGGQKQS GYGKDMSLYG LEDYTLVRHI MVKH
 
 
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