ID   ABDH_ECOHS              Reviewed;         474 AA.
AC   A8A002;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   16-JUN-2009, entry version 14.
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=EcHS_A1528;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000802; ABV05856.1; -; Genomic_DNA.
DR   RefSeq; YP_001458239.1; -.
DR   GeneID; 5593192; -.
DR   GenomeReviews; CP000802_GR; EcHS_A1528.
DR   KEGG; ecx:EcHS_A1528; -.
DR   OMA; A8A002; GYYFQPT.
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_1000067392.
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;  50876 MW;  8B677C59B7409E68 CRC64;
     MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP
     KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG
     LAAGEYLEGH TSMIRRDPLG VVASIAPWNY PLMMAAWKLA PALAAGNCVV LKPSEITPLT
     ALKLAELAKD IFPAGVINIL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTASSI
     KRTHMELGGK APVIVFDDAD IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL
     GAAVATLKSG APDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY
     APTLLAGALQ DDAIVQKEVF GPVVSVTLFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR
     VSARLQYGCT WVNTHFMLVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
//