ID ASTD_PHOPR Reviewed; 485 AA. AC Q6LVE5; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 25-NOV-2008, entry version 33. 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=PBPRA0291; OS Photobacterium profundum (Photobacterium sp. (strain SS9)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=74109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., RA Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., RA Romualdi C., Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and RT expression analysis."; RL Science 307:1459-1461(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. 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; CR378663; CAG18730.1; -; Genomic_DNA. DR RefSeq; YP_128532.1; -. DR GeneID; 3123901; -. DR GenomeReviews; CR354531_GR; PBPRA0291. DR KEGG; ppr:PBPRA0291; -. DR NMPDR; fig|298386.1.peg.2516; -. DR HOGENOM; Q6LVE5; -. DR BioCyc; PPRO298386:PBPRA0291-MON; -. DR GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenas...; IEA:InterPro. 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_DHase_CS. DR InterPro; IPR016162; Ald_DHase_N. DR InterPro; IPR015590; Aldehyde_DHase. 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 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 1 485 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_0000262409. FT NP_BIND 220 225 NAD (By similarity). FT ACT_SITE 243 243 By similarity. FT ACT_SITE 278 278 By similarity. SQ SEQUENCE 485 AA; 51848 MW; 0CF9CA7994567463 CRC64; MTQWIAGNWL AGKGEAMNSL NPFSSEEIWQ GDAATAEQVE QAVSAAREAL TTWRKTDLSE RQAVVEKFAE LVKEHSEHIA HTIAEETGKP LWETRTEAGA MVGKIAISLR AYHERTGEKQ KDIAGTAAVL RHRPLGVMAV FGPYNFPGHL PNGHIVPALL SGNTVVFKPS ELTPKVAQET MKLWEQAGLP KGVLNMVQGA RPTGEALAGS KGIDGLLFTG SANTGHILHR QYAGQPGKML ALEMGGNNPM VISKSYGELD ATVYTIIQSA FISAGQRCTC ARRLYLPQGI EGDAILNRLV EATAKIRIGG PFAEPQPFMG PQISERAADG IIAAQANLVS LGGEVLLEAI RGQGAIVSPA IIEVSNVAEL PDEEYFGPLL QVVRYQDLPD AVELANDTRY GLSAGLVSTD DSEWQYFIDN IRAGIVNRNR QLTGASGDAP FGGPGASGNL RPSAYYAADY CAYPMASMEG EQTELPAQLS PGIAL //