ID ASTD_ENT38 Reviewed; 495 AA. AC A4W9J7; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 16-JUN-2009, entry version 19. 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=Ent638_1698; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; 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., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., RA Vangronsveld J., van der Lelie D., Richardson P.; RT "Complete sequence of chromosome of Enterobacter sp. 638."; RL Submitted (APR-2007) 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; CP000653; ABP60377.1; -; Genomic_DNA. DR RefSeq; YP_001176428.1; -. DR GeneID; 5112437; -. DR GenomeReviews; CP000653_GR; Ent638_1698. DR KEGG; ent:Ent638_1698; -. DR NMPDR; fig|399742.4.peg.1674; -. DR OMA; A4W9J7; KAYHART. 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 1 495 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_1000065756. FT NP_BIND 220 225 NAD (By similarity). FT ACT_SITE 243 243 By similarity. FT ACT_SITE 277 277 By similarity. SQ SEQUENCE 495 AA; 53142 MW; E72D3DEEA16BF24A CRC64; MSLWINGDWV TGEGERRVKT NPVGNEALWQ GFDASPAQVE QACQAARKAF PAWAKLPFTA RQAIVEKFAT LLEANKAELT RVIARETGKP RWEATTEITA MINKITISVK AYHTRTGEQH TAMADGAATL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTVIFKPS ELTPWSGEAV VKLWEQAGLP PGVLNLVQGG RETGQALSAL SDLDGLLFTG SAGTGYQLHR QLAGQPEKIL ALEMGGNNPL IVEDPEDIDA AVHLAIQSAF VTAGQRCTCA RRLLVKNGAQ GDAFLARLIE VTARLVPDAW DAEPQPFIGG LISEQAANNV IHAWREHVAR GAKTLLEPKL VQPGTSLLTP GIIDMSDARD IPDEEVFGPL LCVWRYDDFD SAIAMANNTR YGLSSGLISP DREKFDQLLI EARAGIVNWN KPLTGAASTA PFGGVGASGN HRASAWYAAD YCAWPMASLE TPALTLPEAL NPGLDFTQGN GHESA //