ID   ASTD1_SHEDO             Reviewed;         498 AA.
AC   Q12QD2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            EC=1.2.1.71 {ECO:0000255|HAMAP-Rule:MF_01174};
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            Short=SGSD 1 {ECO:0000255|HAMAP-Rule:MF_01174};
GN   Name=astD1 {ECO:0000255|HAMAP-Rule:MF_01174}; OrderedLocusNames=Sden_1056;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) 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; CP000302; ABE54344.1; -; Genomic_DNA.
DR   RefSeq; WP_011495506.1; NC_007954.1.
DR   AlphaFoldDB; Q12QD2; -.
DR   SMR; Q12QD2; -.
DR   STRING; 318161.Sden_1056; -.
DR   EnsemblBacteria; ABE54344; ABE54344; Sden_1056.
DR   KEGG; sdn:Sden_1056; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; TAGICTD; -.
DR   OrthoDB; 744602at2; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000001982; 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; Reference proteome.
FT   CHAIN           1..498
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase 1"
FT                   /id="PRO_0000262423"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   BINDING         231..236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ   SEQUENCE   498 AA;  52396 MW;  C82E1ABF63CFB1C6 CRC64;
     MNQLEQLTPL TQTQFIAGQW LAGKGPSFSS VNPANGEVIW QGLGADAGQV DAAITSARAA
     FYTWSAMSLT ERLVIVEAFA EQLKEHAELF ARTIALETGK ALWESRTEVG AMTGKIAISI
     KANAERTGTV ENPMPGAKAF IRHKPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVLFKP
     SELTPKVAEL TMQLWQQAGL PNGVLNLLQG EIATGKALAS HKGIDGLFFT GSSNTGHLLH
     QQYAGQPGKI LALEMGGNNP LIITEVANVD AAVHDIIQSA FISSGQRCTC ARRLFIPKTA
     NGDAILAKLL TSTAKIALGD PFAETQPFFG AMISDKAAAG MVKAQADIQA AGGVSLIELT
     QVTPGLGFVT PGIIDVTDAS PLADEEHFGP LLKVYRYTDF DAAIDEANNT SFGLSAGLLA
     DSETDYQHFY RRIRAGIVNW NKPITGASSA APFGGIGASG NHRASAYYAA DYCAYPVSSV
     EAQAVSLPAS LSPGLVIE