ID   ABDH_ECOL6              Reviewed;         474 AA.
AC   Q8FHK7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 49.
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   Name=ydcW; OrderedLocusNames=c1869;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN80331.1; -; Genomic_DNA.
DR   RefSeq; NP_753769.1; -.
DR   HSSP; P56533; 1A4S.
DR   SMR; Q8FHK7; 1-474.
DR   GeneID; 1035695; -.
DR   GenomeReviews; AE014075_GR; c1869.
DR   KEGG; ecc:c1869; -.
DR   HOGENOM; Q8FHK7; -.
DR   OMA; Q8FHK7; QVLRWAN.
DR   BRENDA; 1.2.1.19; 292881.
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_0000269694.
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;  50859 MW;  876ED25B0BE019B9 CRC64;
     MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VNAAVRAADA AFAEWGQTTP
     KARAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG
     LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT
     ALKLAELAKD IFPAGVINVL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTAPSI
     KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL
     GAAVATLKSG SPDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY
     APTLLAGALQ DDAIVQKEVF GPVVSVTLFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR
     VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
//