ASTD_PSEMY
ID ASTD_PSEMY Reviewed; 487 AA.
AC A4XWE7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, 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}; OrderedLocusNames=Pmen_2908;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP85663.1; -; Genomic_DNA.
DR RefSeq; WP_012019089.1; NC_009439.1.
DR AlphaFoldDB; A4XWE7; -.
DR SMR; A4XWE7; -.
DR STRING; 399739.Pmen_2908; -.
DR PRIDE; A4XWE7; -.
DR EnsemblBacteria; ABP85663; ABP85663; Pmen_2908.
DR KEGG; pmy:Pmen_2908; -.
DR PATRIC; fig|399739.8.peg.2947; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
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_1000065761"
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; 51087 MW; 86BBC29E8B4C2CC0 CRC64;
MSTHYIAGQW RPGQGAPLQS LDPVSQAVVW QGQGASAAQV DEAVNAARGA FSLWAAHSLD
GRIAVLERFA AALKSHADEL ARAIGEETGK PLWEAATEVT SMVNKVAISI QSYRERTGEK
SGPLADATAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNCVLFKP SELTPKVAEL
TVKCWIEAGL PAGVLNLLQG GRETGVALAG HPGIDGLFFT GSSRTGNLLH AQFAGRPDKI
LALEMGGNNP LIVDQVADID AAVYTIVQSA FISAGQRCTC ARRLLVPQGQ WGDALLARLV
QVAGQLKVGR FDEQPAPFMG SVISLQAAAQ LMQAQADLLA KGATALLAMT QPQADAALLT
PGILDVTAVS ERPDEEFFGP LLQVIRYSDF DGAIAEANTT AFGLAAGLLS DSKARYEQFW
LHSRAGIVNW NKQLTGAAST APFGGIGASG NHRASAYYAA DYCAYPVASL ESEALTLPTT
LTPGVTL