ID ASTD_SHEHH Reviewed; 486 AA. AC B0TU38; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 25-NOV-2008, entry version 8. 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=Shal_3608; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) 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; CP000931; ABZ78149.1; -; Genomic_DNA. DR RefSeq; YP_001675808.1; -. DR GeneID; 5906268; -. DR GenomeReviews; CP000931_GR; Shal_3608. DR KEGG; shl:Shal_3608; -. 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 1 486 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_1000085407. FT NP_BIND 220 225 NAD (By similarity). FT ACT_SITE 243 243 By similarity. FT ACT_SITE 277 277 By similarity. SQ SEQUENCE 486 AA; 51682 MW; 3930EB1607738049 CRC64; MTQFIEGKWV AGLGHEVTSI NPANQEVIWN SKTATPEQVS QAVDAARNAQ FDWFMLGFEG RLAIVEAYRD QLEANKAEMA EVIAQETGKP QWETATEAGA MIGKIGLSVA AYHKRTGTSE SETPAGRAVL RHKPHGVVAV FGPYNFPGHL PNGHIVPALL AGNTVVFKPS ELTPKVAELM LKLWEKAGLP AGVINLVQGE VETGKALAAH PQIDGLFFTG SSRTGHILHQ QYAGDPGKIL ALEMGGNNPL IIKDVADTKA AVHDIIQSAY ISAGQRCTCA RRLYVEKGAT GDALLEQLVA AIKQIKVGPW NAQPQPFMGS MISETAAKGM VEAQRNLLNL GANSLVELTH IEAGTGLVSP GLIDVTGVIE LPDEEYFGPL LQVVRYSDFD EAIKLANTTR YGLSAGILAD SREDYDYFLA RIRAGIVNWN KQITGASGAA PFGGVGASGN HRASAFYAAD YCAYPVASVE ADAVSLPATL SPGLSL //