ID ASTD_SHEON Reviewed; 487 AA. AC Q8EJ54; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 51. 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=SO_0619; OS Shewanella oneidensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=70863; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MR-1; RX MEDLINE=22297686; PubMed=12368813; DOI=10.1038/nbt749; RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C., RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., RA Clayton R.A., Meyer T., Tsapin A., Scott J., Beanan M.J., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., RA Haft D.H., Kolonay J.F., Madupu R., Peterson J.D., Umayam L.A., RA White O., Wolf A.M., Vamathevan J.J., Weidman J.F., Impraim M., RA Lee K., Berry K.J., Lee C., Mueller J., Khouri H.M., Gill J., RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., RA Venter J.C., Nealson K.H., Fraser C.M.; RT "Genome sequence of the dissimilatory metal ion-reducing bacterium RT Shewanella oneidensis."; RL Nat. Biotechnol. 20:1118-1123(2002). 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; AE014299; AAN53697.1; -; Genomic_DNA. DR RefSeq; NP_716252.1; -. DR HSSP; P51977; 1BXS. DR GeneID; 1168485; -. DR GenomeReviews; AE014299_GR; SO_0619. DR KEGG; son:SO_0619; -. DR NMPDR; fig|211586.1.peg.580; -. DR TIGR; SO_0619; -. DR HOGENOM; Q8EJ54; -. DR OMA; Q8EJ54; SSRTGHL. DR BioCyc; SONE211586:SO_0619-MON; -. DR BRENDA; 1.2.1.71; 257422. 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 1 487 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_0000262426. FT NP_BIND 220 225 NAD (By similarity). FT ACT_SITE 243 243 By similarity. FT ACT_SITE 277 277 By similarity. SQ SEQUENCE 487 AA; 51611 MW; 5215B02398E25232 CRC64; MTHFIKGQWH TGKGHDVASS NPANGEIIWR GQTATAEQVN AAVDAAREAQ FDWFILGFDA RLKIVEAYRS QLEANKAELA ETIAQETGKP QWETATEVAA MIGKIGLSAS AYNKRTGTET NDTPAGRAVL RHKPHGVVAV FGPYNFPGHL PNGHIVPALL AGNSVVFKPS ELTPKVAELM VTLWEKSGLP AGVLNLVQGE VDTGKALASH PQLDGLFFTG SSRTGHLLHQ QYAGHPGKIL ALEMGGNNPL IIKGVADIKA AVHDILQSAY ISSGQRCTCA RRLYVEQGEQ GDALVAKLVE AVKQIKVGPW NAQPQPFMGS MISEAAAKGM VAAQANLLSL GGVPLVELMH LQAGTGLVSP GLIDVTAVSE LPDEEYFGPL LQLVRYSDFD QAIKLANQTR YGLSAGILAD SREDYEYFLA RIRAGIVNWN KQITGASGAA PFGGVGASGN HRASAFYAAD YCAYPVASVE ADAVSLPATL SPGLTLS //