ID   ASTD_PSEPG              Reviewed;         487 AA.
AC   B0KR47;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   16-JUN-2009, entry version 11.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase;
DE            EC=1.2.1.71;
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase;
DE            Short=SGSD;
GN   Name=astD; OrderedLocusNames=PputGB1_3983;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
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., Bruce D., Goodwin L., Chertkov O.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD-dependent reduction of
CC       succinylglutamate semialdehyde into succinylglutamate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: N-succinyl-L-glutamate 5-semialdehyde + NAD(+)
CC       + H(2)O = N-succinyl-L-glutamate + NADH.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 4/5.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC       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; CP000926; ABY99873.1; -; Genomic_DNA.
DR   RefSeq; YP_001670209.1; -.
DR   GeneID; 5871783; -.
DR   GenomeReviews; CP000926_GR; PputGB1_3983.
DR   KEGG; ppg:PputGB1_3983; -.
DR   OMA; B0KR47; EMTQPQA.
DR   GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenas...; IEA:EC.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01174; -; 1.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR017649; SuccinylGlu_semiald_DH_AstD.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   TIGRFAMs; TIGR03240; arg_catab_astD; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    487       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_1000085403.
FT   NP_BIND     221    226       NAD (By similarity).
FT   ACT_SITE    244    244       By similarity.
FT   ACT_SITE    278    278       By similarity.
SQ   SEQUENCE   487 AA;  51375 MW;  FFF2F0F9BFDB7435 CRC64;
     MTTHYIAGNW QAGQGETLQS LNPVTQAVVW QGQGAVASQV DAAVQAARQA FPAWAQLSLE
     ARIDVLEKFA AQLKVHAEAM AQCIGEETGK PLWESATEVT SMINKVAISV QSYRERTGEK
     SGPLADATAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNCVVFKP SELTPKVAEL
     TVNCWIAAGL PAGVLNLVQG ARETGVALAA NPGIDGLFFT GSSRTGNLLH QQFAGRPDKI
     LALEMGGNNP LVVDEVKDLD AAVYTIIQSA FISAGQRCTC ARRLLVPQGS WGDALIARLV
     DVCKTITVGA FDEQPAPFMG SVISLQAARA LIAAQAELAA KGGVKLLEMT QPQADAALLT
     PGIIDVTAVD ERPDEEFFGP LLQVIRYVDF DAAIDEANNT QYGLAAGLLS DSRARYQYFW
     LRSRAGIVNW NKQLTGAASS APFGGVGASG NHRASAYYAA DYCAYPVASL ETASLALPAT
     LTPGVTL
//