ID ASTD_PHOLL Reviewed; 491 AA. AC Q7N2G9; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 25-NOV-2008, entry version 36. 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=plu3108; OS Photorhabdus luminescens subsp. laumondii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Photorhabdus. OX NCBI_TaxID=141679; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TT01; RX MEDLINE=22957627; PubMed=14528314; DOI=10.1038/nbt886; RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., RA Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V., RA Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.; RT "The genome sequence of the entomopathogenic bacterium Photorhabdus RT luminescens."; RL Nat. Biotechnol. 21:1307-1313(2003). 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; BX571869; CAE15482.1; -; Genomic_DNA. DR RefSeq; NP_930340.1; -. DR GeneID; 2803119; -. DR GenomeReviews; BX470251_GR; plu3108. DR KEGG; plu:plu3108; -. DR NMPDR; fig|243265.1.peg.2964; -. DR PhotoList; plu3108; -. DR HOGENOM; Q7N2G9; -. DR BioCyc; PLUM243265:PLU3108-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 1 491 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_0000262410. FT NP_BIND 223 228 NAD (By similarity). FT ACT_SITE 246 246 By similarity. FT ACT_SITE 280 280 By similarity. SQ SEQUENCE 491 AA; 53316 MW; 096BDDC09308DFD5 CRC64; MNYKAHYIGG RWIEGQGESI TKFSPIDQQV LWQANSADAS QVRAACHAAR EAFYAWSHLP ASERIKVIQT FAALLNEEKE TLARVISQET SKPLWETRTE IQSMIGKAAI SIEAWEQRTG ESETIMPDGR ALLRHRPHGV MAVFGPYNFP GHLPNGHIIP ALIAGNTLVF KPSELTPMTA EETVKLWEKA GLPAGVLNLV QGARSTGTAL LEDKQIDGVL FTGSANTGFH FHRMLGGQPE KMLALEMGGN NALIVDAYDD IDAAVYTIVQ SAFISAGQRC TCARRLLVKN GAHGDAVIKR LVEVTERIVP SHWDAQPQPF IGGVISLQAV QNLLEAQDRL QKLGGISLVS LEQCQPQSTL LTPGIIDVSQ VADVPDEEYF GPLLMLMRYD TFDEALAIAN NTRFGLATGL ISPDAALFQR LSEDARAGIV NWNKPLTGAS SKAPFGGIGA SGNYRPSAYY AADYCAWPMA SLVADELTLP ETLAPGLHFP D //