ASTD_PHOLL
ID ASTD_PHOLL Reviewed; 491 AA.
AC Q7N2G9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=plu3108;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571869; CAE15482.1; -; Genomic_DNA.
DR RefSeq; WP_011147324.1; NC_005126.1.
DR AlphaFoldDB; Q7N2G9; -.
DR SMR; Q7N2G9; -.
DR STRING; 243265.plu3108; -.
DR EnsemblBacteria; CAE15482; CAE15482; plu3108.
DR GeneID; 24170073; -.
DR KEGG; plu:plu3108; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR BioCyc; PLUM243265:PLU_RS15475-MON; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000002514; 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; 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; Reference proteome.
FT CHAIN 1..491
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000262410"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT ACT_SITE 280
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT BINDING 223..228
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ SEQUENCE 491 AA; 53316 MW; 096BDDC09308DFD5 CRC64;
MNYKAHYIGG RWIEGQGESI TKFSPIDQQV LWQANSADAS QVRAACHAAR EAFYAWSHLP
ASERIKVIQT FAALLNEEKE TLARVISQET SKPLWETRTE IQSMIGKAAI SIEAWEQRTG
ESETIMPDGR ALLRHRPHGV MAVFGPYNFP GHLPNGHIIP ALIAGNTLVF KPSELTPMTA
EETVKLWEKA GLPAGVLNLV QGARSTGTAL LEDKQIDGVL FTGSANTGFH FHRMLGGQPE
KMLALEMGGN NALIVDAYDD IDAAVYTIVQ SAFISAGQRC TCARRLLVKN GAHGDAVIKR
LVEVTERIVP SHWDAQPQPF IGGVISLQAV QNLLEAQDRL QKLGGISLVS LEQCQPQSTL
LTPGIIDVSQ VADVPDEEYF GPLLMLMRYD TFDEALAIAN NTRFGLATGL ISPDAALFQR
LSEDARAGIV NWNKPLTGAS SKAPFGGIGA SGNYRPSAYY AADYCAWPMA SLVADELTLP
ETLAPGLHFP D