ID   ASTD_ECOL6              Reviewed;         492 AA.
AC   Q8FH01;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 48.
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=c2146;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN80605.1; -; Genomic_DNA.
DR   RefSeq; NP_754040.1; -.
DR   GeneID; 1036571; -.
DR   GenomeReviews; AE014075_GR; c2146.
DR   KEGG; ecc:c2146; -.
DR   NMPDR; fig|199310.1.peg.2083; -.
DR   HOGENOM; Q8FH01; -.
DR   OMA; Q8FH01; SSRTGHL.
DR   BRENDA; 1.2.1.71; 292881.
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    492       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000262401.
FT   NP_BIND     220    225       NAD (By similarity).
FT   ACT_SITE    243    243       By similarity.
FT   ACT_SITE    277    277       By similarity.
SQ   SEQUENCE   492 AA;  52987 MW;  E40838B4D2F8E6E4 CRC64;
     MTLWINGDWV TGQGALRVKR NPVSGEVLWQ GNDADAAQVG QACRAARAAF PRWARLSFGD
     RQVRVERFAG LLESNKAELT AIIARETGKP RWEAATEVTA MINKIAISIK AYHVRTGEQR
     SEMPDGAASL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTIIFKPS ELTPWSGEAV
     MRLWQQAGLP PGVLNLVQGG RATGQALSAL EDLDGLLFTG SANTGYQLHR QLSGQPEKIL
     ALEMGGNNPL IIDEVADIDA AVHLTIQSAF VTAGQRCTCA RRLFLKSGTQ GDAFLARMVA
     VSQRLTPGTW DDEPQPFIGG LISEQAAQQV VTAWQELEAM GGRTLLAPRL LQAGTSLLTP
     GIIEMTGVTG VPDEEVFGPL LRVWRYDNFD EAIRMANNTR FGLSCGLVSP EREKFDQLLL
     GARAGIVNWN KPLTGAASTA PFGGIGASGN HRPSAWYAAD YCAWPMASLE SDSLTLPATL
     NPGLDFSDEV VR
//