ASTD_ECOLI
ID ASTD_ECOLI Reviewed; 492 AA.
AC P76217; P78169; P78170;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase;
DE EC=1.2.1.71 {ECO:0000305|PubMed:15808744, ECO:0000305|PubMed:9696779};
DE AltName: Full=Succinylglutamic semialdehyde dehydrogenase;
DE Short=SGSD;
GN Name=astD; Synonyms=ydjU; OrderedLocusNames=b1746, JW5282;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, INDUCTION, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=9696779; DOI=10.1128/jb.180.16.4278-4286.1998;
RA Schneider B.L., Kiupakis A.K., Reitzer L.J.;
RT "Arginine catabolism and the arginine succinyltransferase pathway in
RT Escherichia coli.";
RL J. Bacteriol. 180:4278-4286(1998).
RN [5]
RP INDUCTION.
RX PubMed=12003934; DOI=10.1128/jb.184.11.2940-2950.2002;
RA Kiupakis A.K., Reitzer L.;
RT "ArgR-independent induction and ArgR-dependent superinduction of the
RT astCADBE operon in Escherichia coli.";
RL J. Bacteriol. 184:2940-2950(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
CC -!- FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate
CC semialdehyde into succinylglutamate (Probable). Also shows in vitro
CC activity with decanal or succinic semialdehyde as the electron donor
CC and NAD as the electron acceptor. No activity is detected with NADP as
CC the electron acceptor. Therefore, is an aldehyde dehydrogenase with
CC broad substrate specificity (PubMed:15808744).
CC {ECO:0000269|PubMed:15808744, ECO:0000305|PubMed:9696779}.
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:0000305|PubMed:15808744, ECO:0000305|PubMed:9696779};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10813;
CC Evidence={ECO:0000305|PubMed:9696779};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanal + H2O + NAD(+) = decanoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:44104, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:31457, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:15808744};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:15808744};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=91 uM for decanal {ECO:0000269|PubMed:15808744};
CC KM=160 uM for NAD (at pH 8.5) {ECO:0000269|PubMed:15808744};
CC KM=1.72 mM for succinic semialdehyde (at pH 8.5)
CC {ECO:0000269|PubMed:15808744};
CC Vmax=5.0 umol/min/mg enzyme with decanal as substrate
CC {ECO:0000269|PubMed:15808744};
CC Vmax=0.69 umol/min/mg enzyme with succinic semialdehyde as substrate
CC {ECO:0000269|PubMed:15808744};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 4/5.
CC {ECO:0000269|PubMed:9696779}.
CC -!- INTERACTION:
CC P76217; P06722: mutH; NbExp=2; IntAct=EBI-545161, EBI-545170;
CC -!- INDUCTION: By nitrogen starvation, and arginine. Induced at stationary
CC phase by sigma S. {ECO:0000269|PubMed:12003934,
CC ECO:0000269|PubMed:9696779}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74816.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15538.2; -; Genomic_DNA.
DR PIR; B64934; B64934.
DR RefSeq; NP_416260.1; NC_000913.3.
DR RefSeq; WP_000177206.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P76217; -.
DR SMR; P76217; -.
DR BioGRID; 4262236; 13.
DR DIP; DIP-9186N; -.
DR IntAct; P76217; 1.
DR STRING; 511145.b1746; -.
DR jPOST; P76217; -.
DR PaxDb; P76217; -.
DR PRIDE; P76217; -.
DR EnsemblBacteria; AAC74816; AAC74816; b1746.
DR EnsemblBacteria; BAA15538; BAA15538; BAA15538.
DR GeneID; 946260; -.
DR KEGG; ecj:JW5282; -.
DR KEGG; eco:b1746; -.
DR PATRIC; fig|1411691.4.peg.510; -.
DR EchoBASE; EB3753; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_6; -.
DR InParanoid; P76217; -.
DR OMA; AWARQPF; -.
DR PhylomeDB; P76217; -.
DR BioCyc; EcoCyc:SUCCGLUALDDEHYD-MON; -.
DR BioCyc; MetaCyc:SUCCGLUALDDEHYD-MON; -.
DR BRENDA; 1.2.1.3; 2026.
DR UniPathway; UPA00185; UER00282.
DR PRO; PR:P76217; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:EcoCyc.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IEA:RHEA.
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 1: Evidence at protein level;
KW Arginine metabolism; NAD; Oxidoreductase; Reference proteome;
KW Stress response.
FT CHAIN 1..492
FT /note="N-succinylglutamate 5-semialdehyde dehydrogenase"
FT /id="PRO_0000056569"
FT ACT_SITE 243
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
FT BINDING 220..225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 492 AA; 53026 MW; CA01ACE48D9CA8DB CRC64;
MTLWINGDWI TGQGASRVKR NPVSGEVLWQ GNDADAAQVE QACRAARAAF PRWARLSFAE
RHAVVERFAA LLESNKAELT AIIARETGKP RWEAATEVTA MINKIAISIK AYHVRTGEQR
SEMPDGAASL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTIIFKPS ELTPWSGEAV
MRLWQQAGLP PGVLNLVQGG RETGQALSAL EDLDGLLFTG SANTGYQLHR QLSGQPEKIL
ALEMGGNNPL IIDEVADIDA AVHLTIQSAF VTAGQRCTCA RRLLLKSGAQ GDAFLARLVA
VSQRLTPGNW DDEPQPFIGG LISEQAAQQV VTAWQQLEAM GGRPLLAPRL LQAGTSLLTP
GIIEMTGVAG VPDEEVFGPL LRVWRYDTFD EAIRMANNTR FGLSCGLVSP EREKFDQLLL
EARAGIVNWN KPLTGAASTA PFGGIGASGN HRPSAWYAAD YCAWPMASLE SDSLTLPATL
NPGLDFSDEV VR
