ID   ASTD_IDILO              Reviewed;         489 AA.
AC   Q5QVX3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
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=IL2316;
OS   Idiomarina loihiensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=135577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-TR / ATCC BAA-735 / DSM 15497;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S.,
RA   Campbell S., Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV83148.1; -; Genomic_DNA.
DR   RefSeq; YP_156697.1; -.
DR   GeneID; 3174410; -.
DR   GenomeReviews; AE017340_GR; IL2316.
DR   KEGG; ilo:IL2316; -.
DR   NMPDR; fig|283942.3.peg.2303; -.
DR   HOGENOM; Q5QVX3; -.
DR   OMA; Q5QVX3; FAPLLQV.
DR   BioCyc; ILOI283942:IL2316-MON; -.
DR   BRENDA; 1.2.1.71; 280818.
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    489       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000262404.
FT   NP_BIND     223    228       NAD (By similarity).
FT   ACT_SITE    246    246       By similarity.
FT   ACT_SITE    280    280       By similarity.
SQ   SEQUENCE   489 AA;  53046 MW;  A431DCD1D149BDFF CRC64;
     MTNSIQFIDG CWEAGEGQLF KSIDPARNEV IWSGEAASET QVEKAILAAR AAFPDWSGRS
     VEERLAICQK FSELLEENKE HLARTMAKET GKPVWETRTE VGAMMGKVAI SERAYHERTG
     TVENDMPGAK AFIRHKPHGV VAVYGPYNFP GHLPNGHIVP ALIAGNTVVF KPSELTPMVA
     QETVKLWEKA GIPAGVLNLV QGEVDTGKAL SAHPQIDGLY FTGSSNTGHL LHKQFGGRPD
     KILALEMGGN NPLLVTNVAD VDAAVHNIVQ SAFITSGQRC TCARRLFIED SEQGRAVLER
     LIEVTENILV DDYEADPQPF MGAMISAKAA GEMVDAQNEL LHKGAKSLVR MKQTDSKKGF
     VTPGIVDVTG VEDLPDEEHF GPLLKVYRFK DIDAAIKEAN NTRYGLSAGV LCDDEQTYRY
     FFKHIRAGIV NWNKPITGAS SAAPFGGIGA SGNHRASAYY AADYCAYPVA SVEADSMSLP
     ESLAPGLKF
//