ID   ABDH_SALTY              Reviewed;         474 AA.
AC   Q8ZPC9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 46.
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=STM1597;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
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; AE008770; AAL20515.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_460556.2; -.
DR   HSSP; P05091; 1O02.
DR   SMR; Q8ZPC9; 1-474.
DR   GeneID; 1253115; -.
DR   GenomeReviews; AE006468_GR; STM1597.
DR   KEGG; stm:STM1597; -.
DR   NMPDR; fig|99287.1.peg.1546; -.
DR   HOGENOM; Q8ZPC9; -.
DR   BioCyc; STYP99287:STM1597-MON; -.
DR   BRENDA; 1.2.1.19; 2.
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_0000269700.
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;  51191 MW;  69A772AC65753601 CRC64;
     MQYQLLINGV LVDGEGERQS VYNPATGEVI LEIAEASPAQ VDAAVQAADN AFAEWGQTTP
     KARAECLLKL ADSIEQNALE FARLESQNCG KPLHCVINDE IPAIVDVFRF FAGAARCLSG
     LAAGEYLEGH TSMIRRDPIG VVASIAPWNY PLMMAAWKLA PALAAGNCVV IKPSEITPLT
     ALKLAVLAKD IFPPGVLNVL FGRGQTVGDV LTGHEKVRMV SLTGSIATGE HILRHTAPAI
     KRTHMELGGK APVIVFDDAD LDAVAQGVRT FGFYNAGQDC TAACRIYAQR GIYDALVEKL
     GNAVSSLKMG APEDESTELG PLSSLAHLKR VTAAVEEAKA LSHIRVITGG SQTEGKGYYF
     APTLLADAKQ EDAIVQREVF GPVVSITVFD DEDQVLRWAN DSRYGLASSV WTQDVGRAHR
     LSARLQYGCT WINTHFMLVS EMPHGGQKQS GYGKDMSLYG LEDYTLVRHI MVKH
//