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ABDH_SALPA
ID   ABDH_SALPA              Reviewed;         474 AA.
AC   Q5PHV8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 99.
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=SPA1271;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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=AAV77220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000026; AAV77220.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q5PHV8; -.
DR   SMR; Q5PHV8; -.
DR   EnsemblBacteria; AAV77220; AAV77220; SPA1271.
DR   KEGG; spt:SPA1271; -.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   UniPathway; UPA00188; UER00292.
DR   Proteomes; UP000008185; 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_0000269698"
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;  51178 MW;  46373A0205DC51AC CRC64;
     MQYQLLINGV LVDGEGERQS VYNPATGEVI LEIAEASPAQ IDAAVQAAVN TFAEWGQTTP
     KARAECLLKL ADSIEQNALE FARLESQNCG KPLHCVINDE IPAIVDVFRF FAGAARCLSG
     LAAGEYLEGH TSMIRRDPIG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT
     ALKLAALAKD IFPPGVLNVL FGRGQTVGDV LTGHEKVRMV SLTGSIATGE HILRHTAPAI
     KRTHMELGGK APVIVFDDAD LDAVAQGVRT FGFYNAGQDC TAACRIYAQR GIYDALVEKL
     GNAVSSLKMG APEDESTELG PLSSLAHLKR VTAAVEEAKA LSHIRVITGG SQTEGKGYYF
     APTLLADAKQ EDAIVQREVF GPVVSITVFD DEDQVLRWGN DSRYGLASSV WTQDVGRAHR
     LSARLQYGCT WINTHFMLVS EMPHGGQKQS GYGKDMSLYG LEDYTLVRHI MVKH
 
 
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