ID   ASTD_PSEA6              Reviewed;         490 AA.
AC   Q15Y60;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=Patl_0649;
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
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   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA   Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-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; CP000388; ABG39178.1; -; Genomic_DNA.
DR   RefSeq; WP_011573541.1; NC_008228.1.
DR   AlphaFoldDB; Q15Y60; -.
DR   SMR; Q15Y60; -.
DR   STRING; 342610.Patl_0649; -.
DR   EnsemblBacteria; ABG39178; ABG39178; Patl_0649.
DR   KEGG; pat:Patl_0649; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; NWNKQLT; -.
DR   OrthoDB; 744602at2; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000001981; 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..490
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT                   /id="PRO_0000262411"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   BINDING         223..228
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ   SEQUENCE   490 AA;  53039 MW;  3D98BACBEAE178E6 CRC64;
     MTQQTHFIAG QWHAGQGHDI ESIDPAKKRQ IWQAKSASSE QVNQAVSSAR KATVTWAACT
     FEQRLAYVKR FGELLAENKD MLALTIAQET GKPLWETATE VGAMMGKIGI SERAYQERTG
     LVENPMPVGK AFIRHKPHGV VAVFGPYNFP GHLPNGHIVP ALLAGNCIVF KPSDLTPLVA
     ERTVQLWEKA GLPKGVLNLV QGEVETGKAL AAHPDLDGLF FTGSSRTGKI LHEQYAGHPG
     KILALEMGGN NPLIVKDISD IDATVHDIIQ SAFVTSGQRC TCARKLFLEN NTQGDAILAR
     LIEVTKNIKV GDYDADEQPF MGAMISKNAA HAMVMAQQQL LDLGATSLVE LTHLDPESGF
     VSPGIIDVTA MVEQMPDDEH FGPLLKVVRF DDFDRAISLG NNTKFGLSAG LLSDSEDLYQ
     HFYQRIRAGI VNWNRPITGA SGAAPFGGVG ESGNHRASAY YAADYCAYPV ASVELEKVTL
     PGNLNPGLNF