ID   ASTD_BURCH              Reviewed;         487 AA.
AC   A0K608;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Bcen2424_1183;
OS   Burkholderia cenocepacia (strain HI2424).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI2424;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA   Konstantinidis K., Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424.";
RL   Submitted (AUG-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; CP000458; ABK07935.1; -; Genomic_DNA.
DR   RefSeq; WP_011544988.1; NC_008542.1.
DR   AlphaFoldDB; A0K608; -.
DR   SMR; A0K608; -.
DR   KEGG; bch:Bcen2424_1183; -.
DR   HOGENOM; CLU_005391_1_0_4; -.
DR   OMA; NWNKQLT; -.
DR   OrthoDB; 744602at2; -.
DR   UniPathway; UPA00185; UER00282.
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..487
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT                   /id="PRO_1000065747"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   BINDING         221..226
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ   SEQUENCE   487 AA;  51721 MW;  D7DA5CEE6743CFCA CRC64;
     MTELFIDGAW VAGSGPVFAS RNPGTDAVAW QGESASAADV DRAVASARRA FAGWSALDFE
     ARCEIVKRFA ALLTERKEAI ATAIGRETGK PLWEARTEVA SMAAKVGISI QAYQERTGEK
     RQDMADGVAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVVFKP SELAPGVARA
     TVEVWQEAGL PAGVLNLVQG EKDTGIALAN HRQIDGLFFT GSSDTGTLLH KQFGGRPEIV
     LALEMGGNNP LVIGEVEDID AAVHHTIQSA FLSAGQRCTC ARRIFVPQGA FGDRFLARFA
     DVTSKITADV FDADPQPFMG AVISARAAAK LVDAQARLVE QGAKPIVAMA QRDPRLGFVN
     AAIVDVTGVA NLPDEEHFGP LAQVVRYATF DEAIERANDT AFGLSAGLLA DDAKVWEHFR
     RTIRAGIVNW NRPTNGASSA APFGGTGRSG NHRPSAYYAA DYCAYPMASV ESTQLTLPAS
     LSPGLHF