ID ASTD_SHIF8 Reviewed; 492 AA. AC Q0T4V3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 26. 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=SFV_1474; OS Shigella flexneri serotype 5b (strain 8401). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=373384; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16822325; DOI=10.1186/1471-2164-7-173; RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., RA Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., RA Jin Q.; RT "Complete genome sequence of Shigella flexneri 5b and comparison with RT Shigella flexneri 2a."; RL BMC Genomics 7:173-173(2006). 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; CP000266; ABF03662.1; -; Genomic_DNA. DR RefSeq; YP_688967.1; -. DR GeneID; 4208100; -. DR GenomeReviews; CP000266_GR; SFV_1474. DR KEGG; sfv:SFV_1474; -. DR HOGENOM; Q0T4V3; -. DR OMA; Q0T4V3; KAYHART. DR BioCyc; SFLE373384:SFV_1474-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 1 492 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_1000065769. FT NP_BIND 220 225 NAD (By similarity). FT ACT_SITE 243 243 By similarity. FT ACT_SITE 277 277 By similarity. SQ SEQUENCE 492 AA; 52978 MW; CD261B3BAF137CDB CRC64; MTLWINGDWI TGQGASRVKR NPVSGEVLWQ GNDADAAQVE QACRAARAAF PRWARLSLAE RQVVVERFAG LLESNKAELT AIIARETGKP RWEAATEVTA MINKIAISIK AYHVRTGEQR SEMPDGAASL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTIIFKPS ELTPWSGEAV MRLWQQAGLP PGVLNLVQGG RETGQALSAL EDLDGLLFTG SANTGYQLHR QLSGQPEKIL ALEMGGNNPL IIDEVADIDA AVHLTIQSAF VTAGQRCTCA RRLLLKSGAQ GDAFLASLVA VSQRLTPGNW DDEPQPFIGG LISEQAAQQV VTAWQQLEAM GGRTLLAPRL LQAGTSLLTP GIIEMTGVGG VPDEEVFGPL LRVWRYDTFD EAIRMANNTR FGLFCGLVSP EREKFDQLLL EARAGIVNWN KPLTGAASTA PFGGIGASGN HRPSAWYAAD YCAWPMASLE SDSLTLPATL NPGLDFSDEV VR //