ID ASTD_BURCM Reviewed; 487 AA. AC Q0BGV0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 25. 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=Bamb_1064; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; 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., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-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; CP000440; ABI86623.1; -; Genomic_DNA. DR RefSeq; YP_772957.1; -. DR GeneID; 4311245; -. DR GenomeReviews; CP000440_GR; Bamb_1064. DR KEGG; bam:Bamb_1064; -. DR NMPDR; fig|339670.3.peg.1861; -. DR OMA; Q0BGV0; EMTQPQA. 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_1000065748. FT NP_BIND 221 226 NAD (By similarity). FT ACT_SITE 244 244 By similarity. FT ACT_SITE 278 278 By similarity. SQ SEQUENCE 487 AA; 51857 MW; 8FDE0F4B187E059D CRC64; MTELFIDGAW IAGSGPAFAS RNPGTDAIAW QGDSASAADV DRAVASARRA FAGWSALDFE ARCEIVKRFA ALLTERKEAI ATAIGRETGK PLWEARTEVA AMAAKVGISI QAYQERTGEK RQDMADGVAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVVFKP SELAPGVARA TVEVWQEAGL PAGVLNLVQG EKDTGIALAN HRQIDGLFFT GSSDTGTLLH RQFGGRPEIV LALEMGGNNP LVIGEVEDLD AAVHHTIQSA FLSAGQRCTC ARRIFVPQGA FGERFLARLA DVTSKITADV FDADPQPFMG AVISARAAAK LVDAQSRLIE QGAKPIIEMT QRDPRLGFVN ASIIDVTGVA NLPDEEHFGP LAQIVRYATF DEAIERANDT AFGLSAGLLA DDAHAWEHFR RTIRAGIVNW NRPTNGASSA APFGGTGRSG NHRPSAYYAA DYCAYPMASV ESTQLTLPAS LSPGLHF //