ASTD_BURA4
ID ASTD_BURA4 Reviewed; 487 AA.
AC B1YW19;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
GN OrderedLocusNames=BamMC406_1064;
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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; CP001025; ACB63555.1; -; Genomic_DNA.
DR RefSeq; WP_012363447.1; NC_010551.1.
DR AlphaFoldDB; B1YW19; -.
DR SMR; B1YW19; -.
DR EnsemblBacteria; ACB63555; ACB63555; BamMC406_1064.
DR KEGG; bac:BamMC406_1064; -.
DR HOGENOM; CLU_005391_1_0_4; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000001680; Chromosome 1.
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 3: Inferred from homology;
KW Arginine metabolism; NAD; Oxidoreductase.
FT CHAIN 1..487
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_1000138037"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT ACT_SITE 278
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT BINDING 221..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ SEQUENCE 487 AA; 51821 MW; B14578D77D4EDB3A CRC64;
MTELFIDGAW IAGSGPAFAS RNPGTDAIAW QGDSASAADV DRAVASARRA FAGWSALDFE
ARCAIVKRFA ALLTERKEAI ATAIGRETGK PLWEARTEVA AMAAKVGISI QAYQERTGEK
RQDMADGVAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNTVVFKP SELAPGVARA
TVEVWQEAGL PAGVLNLVQG EKDTGIALAN HRQIDGLFFT GSSDTGTLLH KQFGGRPEIV
LALEMGGNNP LVIGEVEDLD AAVHHTIQSA FLSAGQRCTC ARRIFVPQGA FGERFLARFA
DVTSKIMADV FDADPQPFMG AVISARAAAK LVDAQSRLVE QGAKPIIEMT QRDPRLGFVN
ASIIDVTGVA NLPDEEHFGP LAQIVRYATF DEAIERANDT AFGLSAGLLA DDAHAWEHFR
RTIRAGIVNW NRPTNGASSA APFGGTGRSG NHRPSAYYAA DYCAYPMASV ESTQLTLPAS
LSPGLHF