ID   ASTD_SHEFN              Reviewed;         486 AA.
AC   Q07XY1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-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=Sfri_3297;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
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., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA   Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA   Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
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; CP000447; ABI73133.1; -; Genomic_DNA.
DR   RefSeq; YP_751972.1; -.
DR   GeneID; 4280199; -.
DR   GenomeReviews; CP000447_GR; Sfri_3297.
DR   KEGG; sfr:Sfri_3297; -.
DR   NMPDR; fig|318167.10.peg.3166; -.
DR   HOGENOM; Q07XY1; -.
DR   OMA; Q07XY1; 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; 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    486       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000262425.
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;  51484 MW;  A59D5184304EC244 CRC64;
     MTQYIQGQWL AGEGHEINSK NPANGDVIWQ GNTATATQVN AAVDAARAAQ FDWFMLGYEA
     RLAIVEAYRA QLEANKAEIA ETIAQETGKP QWETATEVGA MIGKIALSAK AHDKRTGTET
     NDLPAGRAVL RHKPHGVVAV FGPYNFPGHL PNGHIVPALL AGNTVVFKPS ELTPKVAELM
     LKCWDKAGLP QGVVNLVQGE VETGKALASH PQIDGLFFTG SSRTGHILHE QYAGLPGKIL
     ALEMGGNNPL IVKGVTDTKA AVHDIIQSAY ISSGQRCTCA RRLYIEEGAQ GDALIAELVK
     AIKQIKVGAW NVQPQPFMGS MISETAARGM VAAQATLQSL GGVSLVELVQ VEAGTGLVTP
     GLIDVTKVAE LPDEEYFGPL LQLVRYSDFD QAIHLANATR YGLSAGLLAD SREDYDYFLA
     RIRAGIVNWN KQITGASGAA PFGGVGASGN HRASAFYAAD YCAYPVASME ADAVSLPATL
     SPGLSI
//