ID   ABDH_SHIDS              Reviewed;         474 AA.
AC   Q32FQ5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=SDY_1730;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB61850.1; -; Genomic_DNA.
DR   RefSeq; YP_403341.1; -.
DR   SMR; Q32FQ5; 1-474.
DR   GeneID; 3796294; -.
DR   GenomeReviews; CP000034_GR; SDY_1730.
DR   KEGG; sdy:SDY_1730; -.
DR   NMPDR; fig|216598.1.peg.4344; -.
DR   HOGENOM; Q32FQ5; -.
DR   OMA; Q32FQ5; GYYFQPT.
DR   BioCyc; SDYS300267:SDY_1730-MON; -.
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_0000269701.
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;  50881 MW;  B744AD5D2A467164 CRC64;
     MQHKLLINGE LVSGEGEKQP VYNPATGDVL LEIAEASAEQ VDAAVRAADA AFAEWGQTTP
     KVRAECLLKL ADVIEENGQV FAELESRNCG KPLHSAFNDE IPAIVDVFRF FAGAARCLNG
     LAVGEYLEGH TSMIRRDPLG VVASIAPWNY LLMMAAWKLA PALAAGNCVV LKPSEITPLT
     ALKLAELAKD IFPAGVINVL FGRGKTVGDP LTGHPKVRMV SLTGSIATGE HIISHTAPSI
     KRTHMELGGK APVIVFDDAN IEAVVEGVRT FGYYNAGQDC TAACRIYAQK GIYDTLVEKL
     GAAVATLKSG APDDESTELG PLSSLAHLER VSKAVEEAKA TGHIKVITGG EKRKGNGYYY
     APTLLAGALQ DDAIVQKEVF GPVVSVTPFD NEEQVVNWAN DSQYGLASSV WTKDVGRAHR
     VSARLQYGCT WVNTHFILVS EMPHGGQKLS GYGKDMSLYG LEDYTVVRHV MVKH
//