ASTD_SALTY
ID ASTD_SALTY Reviewed; 492 AA.
AC Q8ZPV0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
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=STM1305;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP INDUCTION.
RX PubMed=10074092; DOI=10.1128/jb.181.6.1934-1938.1999;
RA Lu C.-D., Abdelal A.T.;
RT "Role of ArgR in activation of the ast operon, encoding enzymes of the
RT arginine succinyltransferase pathway in Salmonella typhimurium.";
RL J. Bacteriol. 181:1934-1938(1999).
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 -!- INDUCTION: By nitrogen and carbon starvation, and arginine, via the
CC ArgR and Crp transcriptional regulators. {ECO:0000269|PubMed:10074092}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01174}.
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DR EMBL; AE006468; AAL20230.1; -; Genomic_DNA.
DR RefSeq; NP_460271.1; NC_003197.2.
DR RefSeq; WP_000177268.1; NC_003197.2.
DR AlphaFoldDB; Q8ZPV0; -.
DR SMR; Q8ZPV0; -.
DR STRING; 99287.STM1305; -.
DR PaxDb; Q8ZPV0; -.
DR EnsemblBacteria; AAL20230; AAL20230; STM1305.
DR GeneID; 1252823; -.
DR KEGG; stm:STM1305; -.
DR PATRIC; fig|99287.12.peg.1387; -.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; AWARQPF; -.
DR PhylomeDB; Q8ZPV0; -.
DR BioCyc; SENT99287:STM1305-MON; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000001014; Chromosome.
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 2: Evidence at transcript level;
KW Arginine metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..492
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000262422"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT ACT_SITE 277
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 492 AA; 53017 MW; 2B9DD9F7A475D10F CRC64;
MTLWINGDWI TGQGERRRKT NPVSAEILWQ GNDANAAQVA EACQAARAAF PRWARQPFAA
RQAIVEKFAA LLEAHKAELT EVIARETGKP RWEAATEVTA MINKIAISIK AYHARTGAQK
SELVDGAATL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTLIFKPS ELTPWTGETV
IKLWERAGLP AGVLNLVQGG RETGQALSSL DDLDGLLFTG SASTGYQLHR QLSGQPEKIL
ALEMGGNNPL IIEDAANIDA AVHLTLQSAF ITAGQRCTCA RRLLVKQGAQ GDAFLARLVD
VAGRLQPGRW DDDPQPFIGG LISAQAAQHV MEAWRQREAL GGRTLLAPRK VKEGTSLLTP
GIIELTGVAD VPDEEVFGPL LNVWRYAHFD EAIRLANNTR FGLSCGLVST DRAQFEQLLL
EARAGIVNWN KPLTGAASTA PFGGVGASGN HRPSAWYAAD YCAWPMASLE SPELTLPATL
SPGLDFSRRE AV
