ID   ASTD_VIBVU              Reviewed;         485 AA.
AC   Q8DCS9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=VV1_1315;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO09770.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016795; AAO09770.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_043920934.1; NC_004459.3.
DR   AlphaFoldDB; Q8DCS9; -.
DR   SMR; Q8DCS9; -.
DR   PRIDE; Q8DCS9; -.
DR   EnsemblBacteria; AAO09770; AAO09770; VV1_1315.
DR   KEGG; vvu:VV1_1315; -.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; PFMGPQI; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000002275; Chromosome 1.
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..485
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT                   /id="PRO_0000262434"
FT   ACT_SITE        243
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   ACT_SITE        278
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   485 AA;  51885 MW;  B24CCAB434263062 CRC64;
     MTQWIAGEWV EGLGEEFTSL SPYDNQVVWR GKGATAEQVE MAVKAARQAF VGWKTLSVAE
     REAVVLAFAE QVKENSEEIA QVIAKETGKP LWETRTEAAA MAGKIAISIR AYHERTGESQ
     KEAAGNQIVL RHRPLGVMAV FGPYNFPGHL PNGHIVPALL AGNTVVFKPS EQTPWTGELA
     MKLWQAAGLP QGVINLVQGG KETGIALAES KGIDGLLFTG SANTGHLLHR QFAGQPGKML
     ALEMGGNNPM VITDHYGDLD ATVYTIIQSA FISAGQRCTC ARRLYIPLGE KGDALITRLV
     EATKKLRVDQ PFAEPAPFMG PQISVAAANF ILAAQANLQS LGGESLIEAK AGEAAFVTPG
     IIDVTNIAEL PDEEYFGPLL QVVRYQTLEQ AVELANDTRF GLSAGLVSTD DGEWQYFVDH
     IRAGIVNRNR QLTGASGDAP FGGPGASGNL RPSAYYAADY CAYPMASMEG EETSLPATLS
     PGVEL