ID ASTD_BURTA Reviewed; 487 AA. AC Q2SXN9; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 16-JUN-2009, entry version 30. 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=BTH_I1778; OS Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / OS CIP 106301). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., RA Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., RA Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., RA Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J., RA Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., RA Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., RA Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., RA Roberts K., Hatch B., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) 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; CP000086; ABC38809.1; -; Genomic_DNA. DR RefSeq; YP_442310.1; -. DR GeneID; 3849642; -. DR GenomeReviews; CP000086_GR; BTH_I1778. DR KEGG; bte:BTH_I1778; -. DR TIGR; BTH_I1778; -. DR HOGENOM; Q2SXN9; -. DR OMA; Q2SXN9; EMTQPQA. DR BioCyc; BTHA271848:BTH_I1778-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 1 487 N-succinylglutamate 5-semialdehyde FT dehydrogenase. FT /FTId=PRO_0000262392. 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; 51722 MW; C403DA2B5E20965E CRC64; MTELFIDGAW VDGAGPVFAS RNPGTNERVW EGASASADDV ERAVASARRA FAAWSALDLD ARCTIVKRFA ALLVERKEAL ATMIGRETGK PLWEARTEVA SMAAKVDISI TAYHERTGEK RAPMADGVAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVVFKP SELAPGVARA TVEIWRDAGL PAGVLNLVQG EKDTGVALAN HRQIDGLFFT GSSDTGTLLH KQFGGRPEIV LALEMGGNNP LVVAEVEDID AAVHHAIQSA FLSAGQRCTC ARRILVPRGA FGDRFVARLA DVASKITASV FDADPQPFMG AVISARAASR LVAAQARLVG LGASPIIEMK QRDPALGFVN AAILDVTNVR ELPDEEHFGP LAQIVRYTDL DDAIARANDT AFGLSAGLLA DDEQAWHTFR RAIRAGIVNW NRPTNGASSA APFGGAGRSG NHRPSAYYAA DYCAYPMASV ESAQLQMPAS LSPGLHF //