ID   ASTD1_SHEDO             Reviewed;         498 AA.
AC   Q12QD2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-NOV-2008, entry version 24.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase 1;
DE            EC=1.2.1.71;
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase 1;
DE            Short=SGSD 1;
GN   Name=astD1; OrderedLocusNames=Sden_1056;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
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., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-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.
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DR   EMBL; CP000302; ABE54344.1; -; Genomic_DNA.
DR   RefSeq; YP_562067.1; -.
DR   GeneID; 4017563; -.
DR   GenomeReviews; CP000302_GR; Sden_1056.
DR   KEGG; sdn:Sden_1056; -.
DR   NMPDR; fig|318161.14.peg.1038; -.
DR   HOGENOM; Q12QD2; -.
DR   BioCyc; SDEN318161:SDEN_1056-MON; -.
DR   GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenas...; IEA:InterPro.
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    498       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase 1.
FT                                /FTId=PRO_0000262423.
FT   NP_BIND     231    236       NAD (By similarity).
FT   ACT_SITE    254    254       By similarity.
FT   ACT_SITE    288    288       By similarity.
SQ   SEQUENCE   498 AA;  52396 MW;  C82E1ABF63CFB1C6 CRC64;
     MNQLEQLTPL TQTQFIAGQW LAGKGPSFSS VNPANGEVIW QGLGADAGQV DAAITSARAA
     FYTWSAMSLT ERLVIVEAFA EQLKEHAELF ARTIALETGK ALWESRTEVG AMTGKIAISI
     KANAERTGTV ENPMPGAKAF IRHKPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVLFKP
     SELTPKVAEL TMQLWQQAGL PNGVLNLLQG EIATGKALAS HKGIDGLFFT GSSNTGHLLH
     QQYAGQPGKI LALEMGGNNP LIITEVANVD AAVHDIIQSA FISSGQRCTC ARRLFIPKTA
     NGDAILAKLL TSTAKIALGD PFAETQPFFG AMISDKAAAG MVKAQADIQA AGGVSLIELT
     QVTPGLGFVT PGIIDVTDAS PLADEEHFGP LLKVYRYTDF DAAIDEANNT SFGLSAGLLA
     DSETDYQHFY RRIRAGIVNW NKPITGASSA APFGGIGASG NHRASAYYAA DYCAYPVSSV
     EAQAVSLPAS LSPGLVIE
//