ID   ASTD_SHESH              Reviewed;         486 AA.
AC   A8FRE9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   04-NOV-2008, entry version 12.
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=Ssed_0811;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV35422.1; -; Genomic_DNA.
DR   RefSeq; YP_001472550.1; -.
DR   GeneID; 5611705; -.
DR   GenomeReviews; CP000821_GR; Ssed_0811.
DR   KEGG; sse:Ssed_0811; -.
DR   NMPDR; fig|425104.3.peg.717; -.
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_DHase_CS.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR015590; Aldehyde_DHase.
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   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    486       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_1000085409.
FT   NP_BIND     220    225       NAD (By similarity).
FT   ACT_SITE    243    243       By similarity.
FT   ACT_SITE    277    277       By similarity.
SQ   SEQUENCE   486 AA;  51867 MW;  E19CDD8696D85E48 CRC64;
     MTQFIKGQWV AGLGHAVTSK NPANNDVIWN SQTATPEQVN TAVEAAREVQ FDWFMLGFEA
     RLAIVEAYRA QLEENKAEIA ETIAQETGKP QWETATEAGA MIGKIGLSVA AYNKRTGTSE
     NDTPAGRAVL RHKPHGVVAV FGPYNFPGHL PNGHIVPALL AGNTVVFKPS ELTPKVAELM
     LKLWEKAGLP AGVINLVQGE VETGKALASH PQIDGLFFTG SSRTGHILHQ QYAGEPGKIL
     ALEMGGNNPL IIKGVKDSKA AVHDIIQSAY ISSGQRCTCA RRLYVEKGAE GDALLAQLTD
     AVKRIVVGAW NAQPQPFMGA MISETAAKGM VEAQRNLVNL GGHSLVELTH IEEGTGLVSP
     GLIDVSQVIE LPDEEYFGPL LQVVRYTDFD EAIKLANNTR YGLSAGILAD SRDDYEYFLA
     RIRAGIVNWN KQITGASGAA PFGGVGASGN HRASAFYAAD YCAYPVASVE ADEVSLPANL
     SPGLSL
//