ID ASTD_SALPB Reviewed; 492 AA.
AC A9N276;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=SPAB_02038;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-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; CP000886; ABX67425.1; -; Genomic_DNA.
DR RefSeq; WP_000177260.1; NC_010102.1.
DR AlphaFoldDB; A9N276; -.
DR SMR; A9N276; -.
DR KEGG; spq:SPAB_02038; -.
DR PATRIC; fig|1016998.12.peg.1926; -.
DR HOGENOM; CLU_005391_1_0_6; -.
DR BioCyc; SENT1016998:SPAB_RS08320-MONOMER; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000008556; 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 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 NCBIfam; TIGR03240; arg_catab_astD; 1.
DR PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 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..492
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_1000085405"
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; 52992 MW; 6701D88D26BF968F CRC64;
MTLWINGDWI TGQGERRRKT NPVSAEILWQ GNDANAAQVA EACQAARAAF PCWARQPFAA
RQAIVEKFAA LLEAHKADLT EVIARETGKP RWEAATEVTA MINKIAISIK AYHARTGAQK
SELVDGAATL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTLIFKPS ELTPWTGETV
IKLWERAGLP AGVLNLVQGG RETGQALSSL DDLDGLLFTG SASTGYQLHR QLSGQPEKIL
ALEMGGNNPL IIEDVANIDA AVHLTLQSAF ITAGQRCTCA RRLLVKQGAQ GDAFLARLVD
IAGRLQPGRW DDDPQPFIGG LISAQAAQHV MEAWRQREAL GGRTLLAPRK VKEGTSLLTP
GIIELTGVAD VPDEEVFGPL LNVWRYAHFD EAIRLANNTR FGLSCGLVST DRAQFEQLLL
EARAGIVNWN KPLTGAASTA PFGGVGASGN HRPSAWYAAD YCAWPMASLE SPELTLPATL
SPGLDFSRRE AV
//
