ASTD_LEGPL
ID ASTD_LEGPL Reviewed; 495 AA.
AC Q5WVZ4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=lpl1666;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH15906.1; -; Genomic_DNA.
DR RefSeq; WP_011215687.1; NC_006369.1.
DR AlphaFoldDB; Q5WVZ4; -.
DR SMR; Q5WVZ4; -.
DR PRIDE; Q5WVZ4; -.
DR EnsemblBacteria; CAH15906; CAH15906; lpl1666.
DR KEGG; lpf:lpl1666; -.
DR LegioList; lpl1666; -.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; NWNKQLT; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000002517; 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; 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; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; NAD; Oxidoreductase.
FT CHAIN 1..495
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000262405"
FT ACT_SITE 251
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT ACT_SITE 285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT BINDING 228..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ SEQUENCE 495 AA; 54521 MW; DF2B04954B45501C CRC64;
MSKLQIIQSK GQYINGEWIK GNGLILESTN PASGTLLWQG NNATDEEIAN ACYVAHRALK
SWANTSFEER ARYTKAFVEQ VEKNRDQLAR LISLETGKPL WESQTEVSSV IGKVNLSIQA
YQERTWPKQT ETAEANACLR FKPHGVVVVL GAFNFPAHLS NGHIVPALLA GNTVLYKPSE
HTPAVAELII QCWHDSGLPP GVINCLQGNA NCGNTLLSQD IQGVYFTGSY ATGLRIHQQF
CNRPEIILAL EMGGNNPLVI DEVKDIDAAV YHTMLSTMIT AGQRCTCARR IIVPDSQTGD
LFLERFAKAC KLMRIGSFDS QPEPFIGPVI SHVQALKHLH AQKQLVEMGG EIILPMSLLV
EYTGLISPGI IDMTRAKNPP DEEIFAPFAQ IYRYNHFDEA IQLANQTRYG LSAGLLSDNK
DHYLQFYQHI RAGLINWNRP TTGAASSLPF GGVGCSGNHR PSAYFAADYC AYPVASMEQP
LLTTPAQRLP GLVLE