ID G7LMV3_9GAMM Unreviewed; 494 AA.
AC G7LMV3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01174};
DE EC=1.2.1.71 {ECO:0000256|HAMAP-Rule:MF_01174};
DE AltName: Full=Succinylglutamic semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01174};
DE Short=SGSD {ECO:0000256|HAMAP-Rule:MF_01174};
GN Name=astD {ECO:0000256|HAMAP-Rule:MF_01174};
GN ORFNames=BrE312_2340 {ECO:0000313|EMBL:EHD21721.1};
OS Brenneria sp. EniD312.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD21721.1};
RN [1] {ECO:0000313|EMBL:EHD21721.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD21721.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA Glasner J., Perna N., Woyke T.;
RT "Complete sequence of Brenneria sp. EniD312.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate
CC semialdehyde into succinylglutamate. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01174}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01174}.
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DR EMBL; CM001230; EHD21721.1; -; Genomic_DNA.
DR RefSeq; WP_009113023.1; NZ_CM001230.1.
DR AlphaFoldDB; G7LMV3; -.
DR STRING; 598467.BrE312_2340; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000002759; 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 {ECO:0000256|ARBA:ARBA00022503, ECO:0000256|HAMAP-
KW Rule:MF_01174};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01174};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01174}.
FT DOMAIN 12..462
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 246
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 280
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
FT BINDING 223..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
SQ SEQUENCE 494 AA; 52859 MW; 26ED8B642BEBE91E CRC64;
MPSSLLFING AWRQGRGAEF SKTDPLDNQL LWQGAAANAI DIDDACTAAR RAFPAWARLP
LAQRTAVVQR FAGLLEQHKE HLAAVISRET SKPRWETLTE VQAMIGKVGI SLRAYQQRTG
ESRTPMADGA ASLRHRPHGV LAVFGPYNFP GHLPNGHIVP ALLAGNCVVF KASELTPLTA
QETVRLWQQA GLPDGVLNLL QGGRATGAAL AVNPQTDGLL FTGSASTGYQ LHSQLAGQPE
KIIALEMGGN NALIVDEVVE RDAAVNLAIQ SAFISAGQRC TCARRLLVKR GAEGDAFLQR
FIEVARALRI GRWDAEPQPF MGGVISSSAA ENMLVAQQQL LALGATALLT LTRPEANNAL
LTPGILDITG VDGVPDEEYF GPLVRVIRYE DFDEALRIAN QTRYGLAVGL VSPRRDRFDR
LLLEARAGIV NWNKPLTGAS SAAPFGGVGA SGNHRASAFY AADYCAWPMA SLESETLTLP
ATPTPGVSFD TSAE
//
