ID   ASTD2_PSET1             Reviewed;         488 AA.
AC   Q3IC91;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            EC=1.2.1.71 {ECO:0000255|HAMAP-Rule:MF_01174};
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            Short=SGSD 2 {ECO:0000255|HAMAP-Rule:MF_01174};
GN   Name=astD2 {ECO:0000255|HAMAP-Rule:MF_01174}; OrderedLocusNames=PSHAb0426;
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA   Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954247; CAI89463.1; -; Genomic_DNA.
DR   RefSeq; WP_011330051.1; NC_007482.1.
DR   AlphaFoldDB; Q3IC91; -.
DR   SMR; Q3IC91; -.
DR   STRING; 326442.PSHAb0426; -.
DR   EnsemblBacteria; CAI89463; CAI89463; PSHAb0426.
DR   KEGG; pha:PSHAb0426; -.
DR   PATRIC; fig|326442.8.peg.3333; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_6; -.
DR   OMA; TAGICTD; -.
DR   OrthoDB; 744602at2; -.
DR   BioCyc; PHAL326442:PSHA_RS16895-MON; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000006843; Chromosome II.
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..488
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase 2"
FT                   /id="PRO_0000262413"
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   488 AA;  51971 MW;  9A089958B43646BD CRC64;
     MNTQLINNQW QAGQGPAFAS INPSNGETIW QGNGASAEQV NSAIKAARAA QLQWADTPLE
     QRITILENFA AQLKEHSEEF AVIIAQETGK PLWETRTEVG AMTGKVAISV KAYNERTGTT
     ENPMPGAKAF IRHKPHGVVA IFGPYNFPGH LPNGHIVPAI LAGNTVVFKP SELTPHVAQF
     TLSLWLKAGL PAGVINLVQG EIETGKALAA HQDIDGLFFT GSSNTGHLLH KQFAGHPGKI
     LALEMGGNNP LIIKDVNDVS AAVHDIIQSG FITSGQRCTC ARRVFIENSS NGDAILAKLI
     SATKNIVVDD SFATEQPFMG AMISEKAALG MVAAQNELVA KGAEVLVELK QLKPGTGFVS
     PGIIDVTNVN DMPDEEHFGP LIKIYRYSDF DSAINEANNT SFGLSAGLLA DSENDYNHFL
     KRIRAGIVNW NRPITGASSA APFGGIGASG NHRASAYYAA DYCAYPVASV ESDKVTLPQT
     LAPGLIIE