ID ASTD_ACIAD Reviewed; 489 AA. AC Q6FCQ0; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 16-JUN-2009, entry version 38. 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=ACIAD1287; OS Acinetobacter sp. (strain ADP1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., RA Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., RA Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. RT ADP1, a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). 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; CR543861; CAG68159.1; -; Genomic_DNA. DR RefSeq; YP_045981.1; -. DR GeneID; 2880680; -. DR GenomeReviews; CR543861_GR; ACIAD1287. DR KEGG; aci:ACIAD1287; -. DR NMPDR; fig|62977.3.peg.410; -. DR HOGENOM; Q6FCQ0; -. DR OMA; Q6FCQ0; EMTQPQA. DR BioCyc; ASP62977:ACIAD1287-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 1 489 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_0000262386. 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; 52938 MW; 4DE2668956F4F2C1 CRC64; MSHANLWIDG NWVQGQGKSW NTCNPVSQQV VWQGNEATAQ QVEQACEAAR QAFPQWATTS LTDRIAIIER FALLLEQNKE ALAKIISQET SKPLWETLTE VQSMVAKVAI SIRAYHQRTG KSITEMADGA ASLRHRPHGV MAVFGPYNFP GHLPNGHIVP ALIAGNVVVF KPSELTPWTA EATVKLWQQA GLPNAVLNLL QGSRETGIAL AQSEHIDGVL FTGSASTGYQ LHRQLAGAPE KILALEMGGN NALIIEDIDD IDAVVHLAIQ SAFISAGQRC TCARRLIIKN GQAGDAFIQR FIEVARDLVI GDWDAEPQPF MGGVISVKAA EALLKAQQNL IDLGARSLLE MKQLRENSAL VSPAILDVTA VPDIPDEEYF GPLTCIYRYD DFDEALKLAN STRFGLSVGL VSPKRALFER MLIEARAGIV NWNKPLTGAS SAAPFGGVGA SGNHRASAFY AADYCAWPMA SLESEQLSLP EKLSPGIVL //