ID ASTD_SHESA Reviewed; 487 AA. AC A0KST2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 22. 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=Shewana3_0612; OS Shewanella sp. (strain ANA-3). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=94122; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Newman D., Salticov C., Konstantinidis K., Klappenback J., RA Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3."; RL Submitted (SEP-2006) 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; CP000469; ABK46851.1; -; Genomic_DNA. DR RefSeq; YP_868257.1; -. DR GeneID; 4476822; -. DR GenomeReviews; CP000469_GR; Shewana3_0612. DR KEGG; shn:Shewana3_0612; -. DR NMPDR; fig|94122.5.peg.757; -. DR OMA; A0KST2; SSRTGHL. 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; IPR015590; Aldehyde_DH. DR InterPro; IPR017649; SuccinylGlu_semiald_DH_AstD. 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_1000065767. 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; 51561 MW; 9F5C9927B1C03795 CRC64; MTHFIKGQWQ AGKGHDVTSS NPANSEIIWR GQTATAEQVN AAVDAAREAQ FDWFMLGFDG RLKIVEAYRS QLEANKAELA ETIAQETGKP QWETATEVAA MIGKIGLSAT AYNKRTGTEA NDTPAGRAVL RHKPHGVVAV FGPYNFPGHL PNGHIVPALL AGNTVVFKPS ELTPKVAELM VSLWEKAGLP AGVINLVQGE VDTGKALASH PQLDGLFFTG SSRTGHLLHQ QYAGHPGKIL ALEMGGNNPL IIKGVADIKA AVHDILQSAY ISSGQRCTCA RRLYVEQGEQ GDALVAKLVE AVKQIKVGPW NAQPQPFMGS MISEAAAKGM VAAQANLQNL GGVSLVELSH LQAGTGLVSP GLIDVTAVGE LPDEEYFGPL LQLVRYSDFD QAIKLANQTR YGLSAGILAD SRDDYEYFLA RIRAGIVNWN KQITGASGAA PFGGVGASGN HRASAFYAAD YCAYPVASVE ADAVSLPASL SPGLSLE //