ID ASTD_PSEA6 Reviewed; 490 AA. AC Q15Y60; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 25-NOV-2008, entry version 24. 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=Patl_0649; OS Pseudoalteromonas atlantica (strain T6c / BAA-1087). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=342610; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.; RT "Complete sequence of Pseudoalteromonas atlantica T6c."; RL Submitted (JUN-2006) 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; CP000388; ABG39178.1; -; Genomic_DNA. DR RefSeq; YP_660232.1; -. DR GeneID; 4173003; -. DR GenomeReviews; CP000388_GR; Patl_0649. DR KEGG; pat:Patl_0649; -. DR NMPDR; fig|342610.3.peg.2924; -. DR HOGENOM; Q15Y60; -. DR BioCyc; PATL342610:PATL_0649-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 1 490 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_0000262411. FT NP_BIND 223 228 NAD (By similarity). FT ACT_SITE 246 246 By similarity. FT ACT_SITE 280 280 By similarity. SQ SEQUENCE 490 AA; 53039 MW; 3D98BACBEAE178E6 CRC64; MTQQTHFIAG QWHAGQGHDI ESIDPAKKRQ IWQAKSASSE QVNQAVSSAR KATVTWAACT FEQRLAYVKR FGELLAENKD MLALTIAQET GKPLWETATE VGAMMGKIGI SERAYQERTG LVENPMPVGK AFIRHKPHGV VAVFGPYNFP GHLPNGHIVP ALLAGNCIVF KPSDLTPLVA ERTVQLWEKA GLPKGVLNLV QGEVETGKAL AAHPDLDGLF FTGSSRTGKI LHEQYAGHPG KILALEMGGN NPLIVKDISD IDATVHDIIQ SAFVTSGQRC TCARKLFLEN NTQGDAILAR LIEVTKNIKV GDYDADEQPF MGAMISKNAA HAMVMAQQQL LDLGATSLVE LTHLDPESGF VSPGIIDVTA MVEQMPDDEH FGPLLKVVRF DDFDRAISLG NNTKFGLSAG LLSDSEDLYQ HFYQRIRAGI VNWNRPITGA SGAAPFGGVG ESGNHRASAY YAADYCAYPV ASVELEKVTL PGNLNPGLNF //