ID   ASTD_SALTI              Reviewed;         492 AA.
AC   Q8Z6G1; Q7CA95;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 117.
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=STY1809, t1184;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO68840.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD02049.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL513382; CAD02049.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014613; AAO68840.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q8Z6G1; -.
DR   SMR; Q8Z6G1; -.
DR   STRING; 220341.16502886; -.
DR   EnsemblBacteria; AAO68840; AAO68840; t1184.
DR   KEGG; stt:t1184; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; AWARQPF; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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_0000262421"
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;  53212 MW;  037656582563AF41 CRC64;
     MTLWINGDWI TGQGERRRKT NPVSEEILWQ GNDADAAQVA EACQAARAAF PRWARQPFAA
     RQAIVEKFSV LLEAHKADLT EVIARETGKP RWEAATEVTA MINKIAISIK AYHARTGEQK
     SELVDGAATL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTLIFKPS ELTPWTGETV
     IKLWERAGLP AGVLNLVQGG RETGQALSSL DDLDGLLFTG SASTGYQLHR QLSGQPEKIL
     ALEMGGNNPL IIEDATNMDA AVHLTLQSAF ITAGQRCTCA RRLLVKQGAQ GDAFLARLVD
     VAGRLQPGRW DDDPQPFIGG LISAQAAQHV MEAWRQREAL GGRTLLAPRK VKEGTSLLTP
     GIIELTGVAD VPDEEVFGPL LNVWRYAHFD EAIRLANNTR FGLSCGLVST DRAQFEQLLL
     EARAGIVNWN KPLTGAASTA PFGGVGASGN HRPSAWYAAD YCAWPMASLE SPELTLPATL
     SPGLDFSRRE AV