ID A0A1N7RNM2_9BURK Unreviewed; 487 AA.
AC A0A1N7RNM2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ECO:0000313|EMBL:SIT36311.1};
GN ORFNames=BN2476_90005 {ECO:0000313|EMBL:SIT36311.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT36311.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT36311.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT36311.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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; CYGY02000009; SIT36311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7RNM2; -.
DR OrthoDB; 6187633at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000195569; Unassembled WGS sequence.
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 10..461
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 244
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
FT BINDING 221..226
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01174"
SQ SEQUENCE 487 AA; 51836 MW; 352135838C4D988B CRC64;
MSELFIDGEW IAGTGHAFAS RNPGTGATVW EGNSASAEDV DRAVMSARRA FAMWSAVSLD
ERIAIVRRFA ALINERKEAI AEAIGRETGK PLWEACTEAA SMAAKVEISI QSYNERTGER
RAAIADGTAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNAVVFKP SELAPGVARV
TVEVWRDAGL PAGVLNLVQG EKDTGIALAN HRQIDGLFFT GSSDTGTLLH KQFGGRPEIV
LALEMGGNNP LVVAPVADID AAVHHTIQSA FLSAGQRCTC ARRIFVPNDA FGDSFLERLV
DVTSRIAVGE YNADPQPYMG AVISARAAAR LVEAQARLIA DGAKPLLKME QRDPKLGFVT
PAILDVTNVQ SLPDEEHFGP LAQIVRYGSF DEAISGANDT EFGLSAGLLA DDEALWTHFQ
RAIRAGIVNW NRPTNGASSA APFGGTGRSG NNRPSAYYAA DYCAYPMASV ESAQLQMPAS
VSPGLHF
//
