ASTD_LEGPC
ID ASTD_LEGPC Reviewed; 495 AA.
AC A5ICK3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=LPC_1136;
OS Legionella pneumophila (strain Corby).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=400673;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Corby;
RA Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT "Identification and characterization of a new conjugation/ type IVA
RT secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT genomic island.";
RL Submitted (NOV-2006) 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; CP000675; ABQ55103.1; -; Genomic_DNA.
DR RefSeq; WP_011946665.1; NC_009494.2.
DR AlphaFoldDB; A5ICK3; -.
DR SMR; A5ICK3; -.
DR GeneID; 66490837; -.
DR KEGG; lpc:LPC_1136; -.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; NWNKQLT; -.
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; 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_1000065759"
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; 54565 MW; EDD2050525341C6E CRC64;
MSKLQIIQSK GQYINGEWIK GNGLILESTN PASGTLLWQG NNATDEEIAN ACYVAHRALK
SWANTSFEER ARYTKAFVEQ VEKNREQLAR LISLETGKPL WESQTEVSSV IGKVNLSIQA
YQERTWPKQT ETAEANACLR FKPHGIVVVL GAFNFPAHLS NGHIVPALLA GNTVLYKPSE
HTPAVAELII QCWHDSGLPP GVINCLQGNA NCGNTLLSQD IQGVYFTGSY ATGLRIHQQF
CNRPEVILAL EMGGNNPLVI DEVKDIDAAV YHTILSTMIT AGQRCTCARR IIIPDSQTGD
LFLERFAKAC KLMRIGSFDS QPEPFIGPVI SHVQALKHLH AQKQLIEMGG EIILPMSLLL
EYTGLVSPGI IDMTRAKNPP DEEIFAPFAQ IYRYNHFDEA IQLANQTRYG LSAGLLSDNK
DHYQQFYQNI RAGLINWNRP TTGAASSLPF GGVGCSGNHR PSAYFAADYC AYPVASMEQP
LLTTPVQRLP GLVLE