ID   ASTD_BURPS              Reviewed;         487 AA.
AC   Q63SD7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   04-NOV-2026, 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};
GN   OrderedLocusNames=BPSL2387;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate
CC       semialdehyde into succinylglutamate. {ECO:0000255|HAMAP-Rule:MF_01174}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-succinyl-L-glutamate 5-semialdehyde + NAD(+) + H2O = N-
CC         succinyl-L-glutamate + NADH + 2 H(+); 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; BX571965; CAH36389.1; -; Genomic_DNA.
DR   RefSeq; WP_004527437.1; NC_006350.1.
DR   AlphaFoldDB; Q63SD7; -.
DR   SMR; Q63SD7; -.
DR   STRING; 272560.BPSL2387; -.
DR   KEGG; bps:BPSL2387; -.
DR   PATRIC; fig|272560.51.peg.3015; -.
DR   eggNOG; COG1012; Bacteria.
DR   OMA; AAAQWWN; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006527; P:L-arginine catabolic process; IEA:InterPro.
DR   CDD; cd07095; ALDH_SGSD_AstD; 1.
DR   FunFam; 3.40.605.10:FF:000010; N-succinylglutamate 5-semialdehyde dehydrogenase; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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   NCBIfam; TIGR03240; arg_catab_astD; 1.
DR   NCBIfam; NF006992; PRK09457.1; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 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..487
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT                   /id="PRO_0000262389"
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;  51839 MW;  DB57627D1A743BA2 CRC64;
     MTELFIDGAW RDGAGPVFAS RNPGTGEPVW EGAGASADDV ERAVASARRA FAAWSALDLD
     ARCAIVKRFA ALLVERKEAL ATMIGRETGK PLWEARTEVA SMAAKVDVSI AAYHERTGER
     RSPTADGVAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVVFKP SELAPGVARA
     TVEIWRDAGL PAGVLNLVQG EKDTGVALAN HRQIDGLFFT GSSDTGTLLH RQFGGRPEIV
     LALEMGGNNP LVVADVEDID AAVHHAIQSA FLSAGQRCTC ARRILVPRGA FGDRFLERFA
     DVASRITADV YDADPQPFMG AVISARAASR LVAAQAKLLE LGAAPIIEMR QRDPALGFVN
     ASILDVTPVR ELPDEEHFGP LAQIVRYTDL DDAIARANDT AFGLSAGLLA DDETVWNTFR
     RAIRAGIVNW NRPTNGASSA APFGGAGRSG NHRPSAYYAA DYCAYPMASV ESAQLQMPAN
     LSPGLHF
//