ID   ASTD_PSE14              Reviewed;         488 AA.
AC   Q48G19;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
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=PSPPH_3518;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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.
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DR   EMBL; CP000058; AAZ37796.1; -; Genomic_DNA.
DR   RefSeq; YP_275666.1; -.
DR   GeneID; 3560463; -.
DR   GenomeReviews; CP000058_GR; PSPPH_3518.
DR   KEGG; psp:PSPPH_3518; -.
DR   NMPDR; fig|264730.3.peg.3417; -.
DR   HOGENOM; Q48G19; -.
DR   OMA; Q48G19; 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    488       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000262417.
FT   NP_BIND     221    226       NAD (By similarity).
FT   ACT_SITE    244    244       By similarity.
FT   ACT_SITE    278    278       By similarity.
SQ   SEQUENCE   488 AA;  51455 MW;  D14DE7FC1E31F294 CRC64;
     MSTLYIAGAW QAGQGELFHS LNPVSQQTLW SGQAATPEQV DYAVQAARQA FPGWAQRSLD
     QRIAVLEAFA ASLKGRADEL AHCIGEETGK PLWESATEVT SMVNKIAISV QSYRERTGEK
     SGPLGDATAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNTVVFKP SELTPKVAEL
     TVKCWIEAGL PAGVLNLLQG GRETGIALAA NPGIDGLFFT GSSRTGDALH QQFAGRPDKI
     LALEMGGNNP LIVDQVQDIE AAVYNIIQSA FISAGQRCTC ARRLLVPEGD WGDALLARLV
     AVSATIEVGA FDQQPSPFMG SVISLEAAHA LLDAQRNLLA NGAVTLLEMR QPQAGAALLT
     PGIINVSAVA ERPDEELFGP LLQVIRYAGF DAAIAEANAT RYGLAAGLLS DSEARYQQFW
     LHSRAGIVNW NKQLTGAASS APFGGVGASG NHRASAYYAA DYCAYPVASL EAGSLTLPST
     LTPGIRLS
//