ID ASTD_PSEPF Reviewed; 488 AA. AC Q3K885; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 16-JUN-2009, entry version 35. 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=Pfl01_4282; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., RA Larimer F., Land M., Kyripides N., Anderson I., Richardson P.; RT "Complete sequence of Pseudomonas fluorescens PfO-1."; RL Submitted (AUG-2005) 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; CP000094; ABA76019.1; -; Genomic_DNA. DR RefSeq; YP_350010.1; -. DR GeneID; 3712894; -. DR GenomeReviews; CP000094_GR; Pfl01_4282. DR KEGG; pfo:Pfl01_4282; -. DR HOGENOM; Q3K885; -. DR OMA; Q3K885; KAYHART. DR BioCyc; PFLU205922:PFL_4282-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_0000262415. 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; 51250 MW; 47B5200E919D5862 CRC64; MNSLYIAGEW LAGQGEAFQS LNPVTQQVLW SGEGATAAQV ESAVQAARQA FPGWARRTLE DRISVLEAFA AALKNHADEL ARTIGEETGK PLWEAATEVT SMVNKIAISV QSYRERTGEK SGPLGDATAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNSVLFKP SELTPKVAEL TVKCWIEAGL PAGVLNLLQG ARETGIALAA NPGIDGLFFT GSSRTGNHLH QQFAGRPDKI LALEMGGNNP LVVDQVADID AAVYTIIQSA FISAGQRCTC ARRLLVPEGA WGDSLLKRLV EVSSTIEVGA FDQQPAPFMG SVVSLGAAKA LMDAQAHLLA NGAVSLLAMT QPQAQSALLT PGIVDVTAVA DRSDEELFGP LLQVIRYADF AAAIAEANDT AFGLAAGLLS DSEERYQQFW LESRAGIVNW NKQLTGAASS APFGGVGASG NHRASAYYAA DYCAYPVASL ETPSLVLPAA LTPGVKMA //