ID   ABDH_ENT38              Reviewed;         474 AA.
AC   A4WAR9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Gamma-aminobutyraldehyde dehydrogenase;
DE            EC=1.2.1.19;
DE   AltName: Full=1-pyrroline dehydrogenase;
DE   AltName: Full=4-aminobutanal dehydrogenase;
DE            Short=ABALDH;
GN   OrderedLocusNames=Ent638_2124;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Enterobacter sp. 638.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of 1-pyrroline, which is
CC       spontaneously formed from 4-aminobutanal, leading to 4-
CC       aminobutanoate (GABA) (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4-aminobutanal + NAD(+) + H(2)O = 4-
CC       aminobutanoate + NADH.
CC   -!- PATHWAY: Amine and polyamine degradation; putrescine degradation;
CC       4-aminobutanoate from 4-aminobutanal: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- MISCELLANEOUS: 4-aminobutanal is also called gamma-
CC       aminobutyraldehyde.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. Gamma-
CC       aminobutyraldehyde dehydrogenase subfamily.
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DR   EMBL; CP000653; ABP60799.1; -; Genomic_DNA.
DR   RefSeq; YP_001176850.1; -.
DR   GeneID; 5113705; -.
DR   GenomeReviews; CP000653_GR; Ent638_2124.
DR   KEGG; ent:Ent638_2124; -.
DR   NMPDR; fig|399742.4.peg.2072; -.
DR   OMA; A4WAR9; QVLRWAN.
DR   GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:HAMAP.
DR   GO; GO:0016646; F:oxidoreductase activity, acting on the CH-N...; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009447; P:putrescine catabolic process; IEA:HAMAP.
DR   HAMAP; MF_01275; -; 1.
DR   InterPro; IPR017749; 1-pyrroline_dehydrogenase.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   TIGRFAMs; TIGR03374; ABALDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    474       Gamma-aminobutyraldehyde dehydrogenase.
FT                                /FTId=PRO_1000067394.
FT   NP_BIND     172    175       NAD (By similarity).
FT   NP_BIND     225    231       NAD (By similarity).
FT   ACT_SITE    246    246       By similarity.
FT   ACT_SITE    280    280       Nucleophile (By similarity).
FT   BINDING     146    146       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     209    209       NAD (By similarity).
SQ   SEQUENCE   474 AA;  50905 MW;  46C332B65B30D601 CRC64;
     MQNQLLINGE LVNGEGEKQP VYNPATGEVL LEIAEASAAQ VDAAVRAADR AFSEWGHTTP
     KARAECLLKL ADVIEEHAET FARLESQNCG KPLHCVISDE IPAVVDVFRF FAGAARCLNG
     LAAGEYLEGH TSMIRRDPVG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT
     ALKLAELAKD IFPAGVLNVL FGRGKTVGDP LTGHEKVRMV SLTGSIATGE HIISHTASSI
     KRTHMELGGK APVIVFDDAD IDAVVEGVRT FGFYNAGQDC TAACRIYAQK GIYPQLVEKL
     GAAVATLKTG APEDESTELG PLSSAAHLER VCKAVDEAKA LGHVNVVTGG KKVEGGGYFF
     EPTLLAGAKQ EDAIVQREVF GPVVSMTEFD DEEQVLAWAN DSQYGLASSV WTQDVGRAHR
     MSARLQYGCT WVNTHFMLVS EMPHGGMKLS GYGKDMSVYG LEDYTVIRHV MIKH
//