ID   ASTD_SHIB3              Reviewed;         492 AA.
AC   B2U3C8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01174};
DE            EC=1.2.1.71 {ECO:0000255|HAMAP-Rule:MF_01174};
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01174};
DE            Short=SGSD {ECO:0000255|HAMAP-Rule:MF_01174};
GN   Name=astD {ECO:0000255|HAMAP-Rule:MF_01174};
GN   OrderedLocusNames=SbBS512_E1993;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate
CC       semialdehyde into succinylglutamate. {ECO:0000255|HAMAP-Rule:MF_01174}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-succinyl-L-glutamate 5-semialdehyde + NAD(+) = 2 H(+)
CC         + N-succinyl-L-glutamate + NADH; Xref=Rhea:RHEA:10812,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58520, ChEBI:CHEBI:58763; EC=1.2.1.71;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01174};
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 4/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01174}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01174}.
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DR   EMBL; CP001063; ACD09547.1; -; Genomic_DNA.
DR   RefSeq; WP_000177217.1; NC_010658.1.
DR   AlphaFoldDB; B2U3C8; -.
DR   SMR; B2U3C8; -.
DR   STRING; 344609.SbBS512_E1993; -.
DR   PRIDE; B2U3C8; -.
DR   EnsemblBacteria; ACD09547; ACD09547; SbBS512_E1993.
DR   KEGG; sbc:SbBS512_E1993; -.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; AWARQPF; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000001030; Chromosome.
DR   GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR   GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR   CDD; cd07095; ALDH_SGSD_AstD; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_01174; Aldedh_AstD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR017649; SuccinylGlu_semiald_DH_AstD.
DR   PANTHER; PTHR11699:SF197; PTHR11699:SF197; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 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; NAD; Oxidoreductase.
FT   CHAIN           1..492
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT                   /id="PRO_1000138063"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   BINDING         220..225
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ   SEQUENCE   492 AA;  53115 MW;  C6F6C45BF5C7876D CRC64;
     MTLWINGDWI TGQGASRVKR NPVSGEVLWQ GNDADAAQVE QACRAARAAF PRWARLSLAE
     RQVVVERFAG LLESNKAELT AIIARETGKP RWEAATEVTA MINKIAISIK AYHVRTGEQR
     SEMPDGAASL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTIIFKPS ELTPWSGEAV
     MRLWQQAGLP PGVLNLVQGG RETGQALSAL EDLDGLLFTG RANTGYQLHR QLSGQPEKIL
     ALEMGGNNPL IIDEVADIDA AVHLTIQSAF VTAGQRCTCA RRLLLKSGAQ GDAFLARLVA
     VSQRLTPGNW DDEPQPFIGG LISEQAAQQV VTAWQQLEAM GGRTLLAPRL LQSETSLLTP
     GIIEMTGVAG VPDEEVFGPL LRVWRYDSFE EAILMANNTR FGLSCGLVSP EREKFDQLLL
     EARAGIVNWN KPLTGAASTA PFGGIGASGN HRPSAWYAAD YCAWPMASLE SDSLTLPATL
     NPGLDFSDEV VR