ID ASTD1_PSEHT Reviewed; 489 AA. AC Q3IFT7; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 04-NOV-2008, entry version 29. DE RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase 1; DE EC=1.2.1.71; DE AltName: Full=Succinylglutamic semialdehyde dehydrogenase 1; DE Short=SGSD 1; GN Name=astD1; OrderedLocusNames=PSHAa0196; OS Pseudoalteromonas haloplanktis (strain TAC 125). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=326442; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16169927; DOI=10.1101/gr.4126905; RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., RA Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., RA Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., RA Danchin A.; RT "Coping with cold: the genome of the versatile marine Antarctica RT bacterium Pseudoalteromonas haloplanktis TAC125."; RL Genome Res. 15:1325-1335(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; CR954246; CAI85299.1; -; Genomic_DNA. DR RefSeq; YP_338742.1; -. DR GeneID; 3708763; -. DR GenomeReviews; CR954246_GR; PSHAa0196. DR KEGG; pha:PSHAa0196; -. DR NMPDR; fig|326442.4.peg.280; -. DR HOGENOM; Q3IFT7; -. DR BioCyc; PHAL326442:PSHAA0196-MON; -. 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 1 489 N-succinylglutamate 5-semialdehyde FT dehydrogenase 1. FT /FTId=PRO_0000262412. FT NP_BIND 223 228 NAD (By similarity). FT ACT_SITE 246 246 By similarity. FT ACT_SITE 280 280 By similarity. SQ SEQUENCE 489 AA; 52132 MW; CA361C82827678A9 CRC64; MTHPAQFING QWSQGQGTEF SSVNPANNNV IFQANSATAE QVDAAVSAAR EAFYAWADKT FAERLEIVKA FAAQLKENSE ELAITIAQET GKPLWETRTE AGAMVGKIAI SEKAFLERTG DVENAMPLGR AMIRHKPHGV VAVFGPYNFP GHLPNGHIVP ALLAGNTVIF KPSELTPKVA ELTLKLWEKA GLPAGVINLV QGEVATGKAL AAHKGIDGLF FTGSSRTGHI LHEQFAGQPG KILALEMGGN NPLIITDVED TKAVVHDIIQ SAFISSGQRC TCARKLFLPT GSKGDVILER LITATKAIKV GNYDDADQPF MGSMISSAAA AGMVKAQNEL VELGAQVLVE LEHTVNTGFV TPGIIECTNI SDFPDEEHFG PLLKVFRFDD FDQAIDKAND TSFGLSAGLL SDSAADYEHF LRRIRAGIVN WNRPITGASS AAPFGGIGAS GNHRASAYYA ADYCAYPVAS VELEKVAMPA TLSPGLKID //