ID ASTD_IDILO Reviewed; 489 AA.
AC Q5QVX3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=IL2316;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV83148.1; -; Genomic_DNA.
DR RefSeq; WP_011235542.1; NC_006512.1.
DR AlphaFoldDB; Q5QVX3; -.
DR SMR; Q5QVX3; -.
DR STRING; 283942.IL2316; -.
DR KEGG; ilo:IL2316; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OrthoDB; 9812625at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000001171; 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; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..489
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000262404"
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 489 AA; 53046 MW; A431DCD1D149BDFF CRC64;
MTNSIQFIDG CWEAGEGQLF KSIDPARNEV IWSGEAASET QVEKAILAAR AAFPDWSGRS
VEERLAICQK FSELLEENKE HLARTMAKET GKPVWETRTE VGAMMGKVAI SERAYHERTG
TVENDMPGAK AFIRHKPHGV VAVYGPYNFP GHLPNGHIVP ALIAGNTVVF KPSELTPMVA
QETVKLWEKA GIPAGVLNLV QGEVDTGKAL SAHPQIDGLY FTGSSNTGHL LHKQFGGRPD
KILALEMGGN NPLLVTNVAD VDAAVHNIVQ SAFITSGQRC TCARRLFIED SEQGRAVLER
LIEVTENILV DDYEADPQPF MGAMISAKAA GEMVDAQNEL LHKGAKSLVR MKQTDSKKGF
VTPGIVDVTG VEDLPDEEHF GPLLKVYRFK DIDAAIKEAN NTRYGLSAGV LCDDEQTYRY
FFKHIRAGIV NWNKPITGAS SAAPFGGIGA SGNHRASAYY AADYCAYPVA SVEADSMSLP
ESLAPGLKF
//
