ID   ASTD_PSEF5              Reviewed;         488 AA.
AC   Q4K837;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-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=PFL_4512;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(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; CP000076; AAY93759.1; -; Genomic_DNA.
DR   RefSeq; YP_261596.1; -.
DR   GeneID; 3478627; -.
DR   GenomeReviews; CP000076_GR; PFL_4512.
DR   KEGG; pfl:PFL_4512; -.
DR   NMPDR; fig|220664.3.peg.5007; -.
DR   HOGENOM; Q4K837; -.
DR   OMA; Q4K837; EMTQPQA.
DR   BioCyc; PFLU220664:PFL_4512-MON; -.
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_0000262414.
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;  51299 MW;  5C4F96D672036DEE CRC64;
     MSTLYIAGQW LAGQGEAFTS VNPVTQAVIW SGNGATAAQV ESAVQAARQA FPAWAKRSLE
     ERISVLEAFA ASLKSRADEL ARCIGEETGK PLWEAATEVT SMVNKIAISV QSYRERTGEK
     SGPLGDATAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNSVLFKP SELTPKVAEL
     TVQCWIEAGL PAGVLNLLQG ARETGIALAA NPGIDGLFFT GSSRTGNHLH QQFAGRPDKI
     LALEMGGNNP LVVEQVADLD AAVYTIIQSA FISAGQRCTC ARRLLVPQGA WGDTLLARLV
     AVSATIEVGA FDQQPAPFMG SVISLGAARA LMDAQQQLLA NGAVALLEMT QPQAQAALLT
     PGILDVSAVA ERPDEELFGP LLQVIRYADF DDAIAEANNT QYGLAAGLLS DSAERYQQFW
     LESRAGIVNW NKQLTGAASS APFGGVGASG NHRASAYYAA DYCAYPVASL ETPSLVLPSA
     LTPGVRLS
//