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Database: UniProt
Entry: ASTD1_CAUVC
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Original site: ASTD1_CAUVC 
ID   ASTD1_CAUVC             Reviewed;         472 AA.
AC   Q9AAL5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            EC=1.2.1.71 {ECO:0000255|HAMAP-Rule:MF_01174};
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            Short=SGSD 1 {ECO:0000255|HAMAP-Rule:MF_01174};
GN   Name=astD1 {ECO:0000255|HAMAP-Rule:MF_01174}; OrderedLocusNames=CC_0582;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK22568.1; -; Genomic_DNA.
DR   PIR; D87321; D87321.
DR   RefSeq; NP_419400.1; NC_002696.2.
DR   RefSeq; WP_010918469.1; NC_002696.2.
DR   AlphaFoldDB; Q9AAL5; -.
DR   SMR; Q9AAL5; -.
DR   STRING; 190650.CC_0582; -.
DR   EnsemblBacteria; AAK22568; AAK22568; CC_0582.
DR   KEGG; ccr:CC_0582; -.
DR   PATRIC; fig|190650.5.peg.594; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_5; -.
DR   BioCyc; CAULO:CC0582-MONOMER; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000001816; 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..472
FT                   /note="N-succinylglutamate 5-semialdehyde dehydrogenase 1"
FT                   /id="PRO_0000262394"
FT   ACT_SITE        232
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
FT   BINDING         209..214
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01174"
SQ   SEQUENCE   472 AA;  49811 MW;  28E7C4A5FF80EF2F CRC64;
     MSASRLISRD PYTGEAIADF AVNDARSIDA ACHSARAAFA EWAMTPLAER RAIALRFAET
     VRARREEIAT LIARETGKPM WEALTEADSV AAKVAISIRA QDERAGERSE PMADATARLA
     HRPHGVLAVI GPFNFPMHLA NGHIVPALLA GNAVVFKPSE KTPACGQLMG ELWRAAGLPD
     HVLTIVIGGG EAGEALVRHE ALDGVLFTGG VQAGRAIHRA LADAPHKILA LELGGNAPLV
     VWDVADIEAA AHLIVQSAYV TAGQRCTCAR RLILPEGARG DALLEALTML MDRLVIGGPF
     QSPAPFMGPV IDAHAAAQVL AAQDRMTADG GRPLRLAAVR EARSALLSPG LIELTDAPLR
     DEEIFGPLLQ VRRAADFDAA LALANATRFG LAAGLISDDE ALYRRFWTSV RAGIVNWNRP
     TTGASSAAPF GGVGGSGNHR PSAYYAADYS AYPVAGLESP SPVYRLPIGL NP
//
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