ASTD_SHEFN
ID ASTD_SHEFN Reviewed; 486 AA.
AC Q07XY1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Sfri_3297;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) 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; CP000447; ABI73133.1; -; Genomic_DNA.
DR RefSeq; WP_011638736.1; NC_008345.1.
DR AlphaFoldDB; Q07XY1; -.
DR SMR; Q07XY1; -.
DR STRING; 318167.Sfri_3297; -.
DR EnsemblBacteria; ABI73133; ABI73133; Sfri_3297.
DR KEGG; sfr:Sfri_3297; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR OMA; PFMGPQI; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00185; UER00282.
DR Proteomes; UP000000684; 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..486
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000262425"
FT ACT_SITE 243
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT ACT_SITE 277
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT BINDING 220..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ SEQUENCE 486 AA; 51484 MW; A59D5184304EC244 CRC64;
MTQYIQGQWL AGEGHEINSK NPANGDVIWQ GNTATATQVN AAVDAARAAQ FDWFMLGYEA
RLAIVEAYRA QLEANKAEIA ETIAQETGKP QWETATEVGA MIGKIALSAK AHDKRTGTET
NDLPAGRAVL RHKPHGVVAV FGPYNFPGHL PNGHIVPALL AGNTVVFKPS ELTPKVAELM
LKCWDKAGLP QGVVNLVQGE VETGKALASH PQIDGLFFTG SSRTGHILHE QYAGLPGKIL
ALEMGGNNPL IVKGVTDTKA AVHDIIQSAY ISSGQRCTCA RRLYIEEGAQ GDALIAELVK
AIKQIKVGAW NVQPQPFMGS MISETAARGM VAAQATLQSL GGVSLVELVQ VEAGTGLVTP
GLIDVTKVAE LPDEEYFGPL LQLVRYSDFD QAIHLANATR YGLSAGLLAD SREDYDYFLA
RIRAGIVNWN KQITGASGAA PFGGVGASGN HRASAFYAAD YCAYPVASME ADAVSLPATL
SPGLSI