ID   ASTD_CHRSD              Reviewed;         489 AA.
AC   Q1QTQ7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=Csal_2805;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
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; CP000285; ABE60151.1; -; Genomic_DNA.
DR   RefSeq; YP_574850.1; -.
DR   GeneID; 4028490; -.
DR   GenomeReviews; CP000285_GR; Csal_2805.
DR   KEGG; csa:Csal_2805; -.
DR   NMPDR; fig|290398.4.peg.2043; -.
DR   HOGENOM; Q1QTQ7; -.
DR   OMA; Q1QTQ7; EMTQPQA.
DR   BioCyc; CSAL290398:CSAL_2805-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    489       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000262397.
FT   NP_BIND     224    229       NAD (By similarity).
FT   ACT_SITE    247    247       By similarity.
FT   ACT_SITE    281    281       By similarity.
SQ   SEQUENCE   489 AA;  51947 MW;  31D102ADFF926682 CRC64;
     MQAKQQLLID GAWVDGDAAR FAKTDPVSGE TLWTATAASA TQVEHAVAAA RQAFPDWARR
     SFAERQAVVE RFRECLETHR EHLATAIAQE TGKPLWEART EVGAMIGKVA ISITAYHERT
     GERARDIGDA RAVLRHRPHG VLAVYGPYNF PGHLPNGHIV PALLAGNAVV FKPSEQTPMT
     ADLTLQCWLE AGLPAGVINL VQGAAEVGQA LAGSADIDGL LFTGSAKVGG LLHRQFGGQV
     DKILALELGG NNPLVVKDVP DREAAVLSIL QSAFASGGQR CTCARRLIVP HGAVGDDLID
     ALTSAIAELR VAAPFSEPAP FYAGLTSVEA ADGLLAAQDD LVARGGRPLS RMRRLQAGTS
     LLSPGLIDVT GCDVPDEEHF GPLLKVHRYR DWDEAIALAN DTRYGLSAGL IGGERADWDD
     FLLRIRAGIV NWNRQTTGAS SDAPFGGIGD SGNHRPSAYY AADYCAYPVA SMEAETLVLP
     ETLPPGVVL
//