ID   ASTD_ENT38              Reviewed;         495 AA.
AC   A4W9J7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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}; OrderedLocusNames=Ent638_1698;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP60377.1; -; Genomic_DNA.
DR   RefSeq; WP_012017093.1; NC_009436.1.
DR   AlphaFoldDB; A4W9J7; -.
DR   SMR; A4W9J7; -.
DR   STRING; 399742.Ent638_1698; -.
DR   PRIDE; A4W9J7; -.
DR   EnsemblBacteria; ABP60377; ABP60377; Ent638_1698.
DR   KEGG; ent:Ent638_1698; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; TAGICTD; -.
DR   OrthoDB; 744602at2; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000000230; 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..495
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT                   /id="PRO_1000065756"
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   495 AA;  53142 MW;  E72D3DEEA16BF24A CRC64;
     MSLWINGDWV TGEGERRVKT NPVGNEALWQ GFDASPAQVE QACQAARKAF PAWAKLPFTA
     RQAIVEKFAT LLEANKAELT RVIARETGKP RWEATTEITA MINKITISVK AYHTRTGEQH
     TAMADGAATL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTVIFKPS ELTPWSGEAV
     VKLWEQAGLP PGVLNLVQGG RETGQALSAL SDLDGLLFTG SAGTGYQLHR QLAGQPEKIL
     ALEMGGNNPL IVEDPEDIDA AVHLAIQSAF VTAGQRCTCA RRLLVKNGAQ GDAFLARLIE
     VTARLVPDAW DAEPQPFIGG LISEQAANNV IHAWREHVAR GAKTLLEPKL VQPGTSLLTP
     GIIDMSDARD IPDEEVFGPL LCVWRYDDFD SAIAMANNTR YGLSSGLISP DREKFDQLLI
     EARAGIVNWN KPLTGAASTA PFGGVGASGN HRASAWYAAD YCAWPMASLE TPALTLPEAL
     NPGLDFTQGN GHESA