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ABDH_ECO8A
ID   ABDH_ECO8A              Reviewed;         474 AA.
AC   B7LZ33;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=ECIAI1_1440;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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 + 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}.
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DR   EMBL; CU928160; CAQ98298.1; -; Genomic_DNA.
DR   RefSeq; WP_001163892.1; NC_011741.1.
DR   AlphaFoldDB; B7LZ33; -.
DR   SMR; B7LZ33; -.
DR   GeneID; 66674705; -.
DR   KEGG; ecr:ECIAI1_1440; -.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; NDDLGEV; -.
DR   UniPathway; UPA00188; UER00292.
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_1000140270"
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;  50846 MW;  2F723041BFAB1A75 CRC64;
     MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP
     KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG
     LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT
     ALKLAELAKD IFPAGVINVL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTASSI
     KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL
     GAAVATLKSG APDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY
     APTLLAGALQ DDAIVQKEVF GPVVSVTPFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR
     VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
 
 
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