ID ASTD_ECOUT Reviewed; 492 AA. AC Q1RB47; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 27. 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=UTI89_C1941; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE07417.1; -; Genomic_DNA. DR RefSeq; YP_540948.1; -. DR GeneID; 3991597; -. DR GenomeReviews; CP000243_GR; UTI89_C1941. DR KEGG; eci:UTI89_C1941; -. DR HOGENOM; Q1RB47; -. DR OMA; Q1RB47; KAYHART. DR BioCyc; ECOL364106:UTI89_C1941-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_0000262399. 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; 53099 MW; F569ABD5AA7D2515 CRC64; MTLWINGDWV TGQGALRVKR NPVSGEVLWQ GNDADAAQVG QACRAARAAF PRWARLSFGD RQVRVERFAG LLESNKAELT AIIARETGKP RWEAATEVTA MINKIAISIK AYHVRTGEQR SEMPDGAASL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTIIFKPS ELTPWSGDAV MRLWQQAGLP PGVLNLVQGG RETGQALSAL EDLDGLLFTG SANTGYQLHR QLSGQPEKIL ALEMGGNNPL IIDEVADIDA AVHLTIQSAF VTAGQRCTCA RRLFLKSGTQ GDAFLARLVA VSQRLTPGTW DDEPQPFIGG LISEQAAQQV VTAWQELEAM GGRTLLAPRL LQAGTSLLTP GIIEMTGVTG LPDEEVFGPL LRVWRYDNFD EAIRMANNTR FGLSCGLVSP EREKFDQLLL EARAGIVNWN KPLTGAASTA PFGGIGASGN HRPSAWYAAD YCAWPMASLE SDSLTLPATL NPGLDFSDEV VR //