ASTD_PSESM
ID ASTD_PSESM Reviewed; 488 AA.
AC Q885J7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, 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}; OrderedLocusNames=PSPTO_1835;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO55354.1; -; Genomic_DNA.
DR RefSeq; NP_791659.1; NC_004578.1.
DR AlphaFoldDB; Q885J7; -.
DR SMR; Q885J7; -.
DR STRING; 223283.PSPTO_1835; -.
DR EnsemblBacteria; AAO55354; AAO55354; PSPTO_1835.
DR KEGG; pst:PSPTO_1835; -.
DR PATRIC; fig|223283.9.peg.1865; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR PhylomeDB; Q885J7; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; ISS:JCVI.
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"
FT /id="PRO_0000262419"
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; 51252 MW; 9FD45FF64E7B8486 CRC64;
MSTLYIAGAW QAGQGELFHS LNPVTLHVLW SGQGATAEQV DHAVQAARQA FPAWALLSLD
QRIAVLDAFA VSLKAHADEL ANCIGEETGK PLWESATEVT SMVNKIAISV QSYRERTGEK
SAPLGDATAV LRHKPHGVVA VFGPYNFPGH LPNGHIVPAL LAGNTVLFKP SELTPKVAEL
TVKCWIEAGL PAGVLNLLQG GRETGIALAA NPGIDGLFFT GSSRTGNALH QQFAGRPDKI
LALEMGGNNP LVVDQVQDID AAVYTIIQSA FISAGQRCTC ARRLLVPEGD WGDALLARLV
AVSATLDVGA FDQQPAPFMG SVISLEAARA LLDAQRHLLA NGAVTLLEMR QPQPGAALLT
PGIVDVSAVA NRPDVELFGP LLQVVRYAGF DAAIAEANAT QYGLAAGLLS DSEARYQQFW
LQSRAGIVNW NKQLTGAASS APFGGVGASG NHRASAYYAA DYCAYPVASL ETGSLTLPAT
LTPGVRLS
