[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.6.363; PubMed=9097039 [NCBI, ExPASy, EBI, Israel, Japan] Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."; DNA Res. 3:363-377(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[4]	INDUCTION, AND PATHWAY. PubMed=9696779 [NCBI, ExPASy, EBI, Israel, Japan] Schneider B.L., Kiupakis A.K., Reitzer L.J.; "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli."; J. Bacteriol. 180:4278-4286(1998).
[5]	INDUCTION. DOI=10.1128/JB.184.11.2940-2950.2002; PubMed=12003934 [NCBI, ExPASy, EBI, Israel, Japan] Kiupakis A.K., Reitzer L.; "ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli."; J. Bacteriol. 184:2940-2950(2002).
[6]	FUNCTION, AND KINETIC PARAMETERS. DOI=10.1016/j.femsre.2004.12.006; PubMed=15808744 [NCBI, ExPASy, EBI, Israel, Japan] Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F.; "Enzyme genomics: application of general enzymatic screens to discover new enzymes."; FEMS Microbiol. Rev. 29:263-279(2005).

Comments

FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. Also shows activity with decanal or succinic semialdehyde as the electron donor and NAD as the electron acceptor. No activity is detected with NADP as the electron acceptor. Therefore, is an aldehyde dehydrogenase with broad substrate specificity.
CATALYTIC ACTIVITY: N-succinyl-L-glutamate 5-semialdehyde + NAD⁺ + H₂O = N-succinyl-L-glutamate + NADH.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=91 µM for decanal;
	K_M=160 µM for NAD (at pH 8.5);
	K_M=1.72 mM for succinic semialdehyde (at pH 8.5);
	V_max=5.0 µmol/min/mg enzyme with decanal as substrate;
	V_max=0.69 µmol/min/mg enzyme with succinic semialdehyde as substrate;

PATHWAY: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 4/5 .
INTERACTION:
P06722:mutH; NbExp=1; IntAct=EBI-545161, EBI-545170;
INDUCTION: By nitrogen starvation, and arginine. Induced at stationary phase by sigma S.
SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U00096; AAC74816.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA15538.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B64934; B64934.

RefSeq

AP_002365.1; -.
NP_416260.1; -.

3D structure databases

ModBase

P76217.

Protein-protein interaction databases

DIP

DIP:9186N; -.

IntAct

P76217; -.

Enzyme and pathway databases

BioCyc

EcoCyc:SUCCGLUALDDEHYD-MON; -.
MetaCyc:SUCCGLUALDDEHYD-MON; -.

Organism-specific databases

EchoBASE

EB3753; -.

EcoGene

EG13997; astD.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

HAMAP

MF_01174; -; 1.
PBIL [Tree]

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR017649; SuccinylGlu_semiald_DH_AstD.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

BLOCKS

P76217.

Genome annotation databases

GeneID

946260; -.

GenomeReviews

U00096_GR; b1746.
AP009048_GR; JW5282.

KEGG

ecj:JW5282; -.
eco:b1746; -.

Phylogenomic databases

HOGENOM

P76217; -.

Genome annotation databases

CMR

P76217; b1746.

Other

ProtoNet

P76217.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Arginine metabolism; Complete proteome; NAD; Oxidoreductase; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 492`	`492`	`N-succinylglutamate 5-semialdehyde dehydrogenase.`	`PRO_0000056569`
`NP_BIND`	`220 225`	`6`	`NAD (By similarity).`
`ACT_SITE`	`243 243`		`By similarity.`
`ACT_SITE`	`277 277`		`By similarity.`

Sequence information

Length: 492 AA [This is the length of the unprocessed precursor]

Molecular weight: 53026 Da [This is the MW of the unprocessed precursor]

CRC64: CA01ACE48D9CA8DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTLWINGDWI TGQGASRVKR NPVSGEVLWQ GNDADAAQVE QACRAARAAF PRWARLSFAE 

        70         80         90        100        110        120 
RHAVVERFAA LLESNKAELT AIIARETGKP RWEAATEVTA MINKIAISIK AYHVRTGEQR 

       130        140        150        160        170        180 
SEMPDGAASL RHRPHGVLAV FGPYNFPGHL PNGHIVPALL AGNTIIFKPS ELTPWSGEAV 

       190        200        210        220        230        240 
MRLWQQAGLP PGVLNLVQGG RETGQALSAL EDLDGLLFTG SANTGYQLHR QLSGQPEKIL 

       250        260        270        280        290        300 
ALEMGGNNPL IIDEVADIDA AVHLTIQSAF VTAGQRCTCA RRLLLKSGAQ GDAFLARLVA 

       310        320        330        340        350        360 
VSQRLTPGNW DDEPQPFIGG LISEQAAQQV VTAWQQLEAM GGRPLLAPRL LQAGTSLLTP 

       370        380        390        400        410        420 
GIIEMTGVAG VPDEEVFGPL LRVWRYDTFD EAIRMANNTR FGLSCGLVSP EREKFDQLLL 

       430        440        450        460        470        480 
EARAGIVNWN KPLTGAASTA PFGGIGASGN HRPSAWYAAD YCAWPMASLE SDSLTLPATL 

       490 
NPGLDFSDEV VR

P76217 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools