Reviewed, UniProtKB/Swiss-Prot P76217 (ASTD_ECOLI)

Names and originHide

Protein names

Recommended name:
N-succinylglutamate 5-semialdehyde dehydrogenase
EC=1.2.1.71

Alternative name(s):
Succinylglutamic semialdehyde dehydrogenase
Short name=SGSD

Gene names

Name:	astD
Synonyms:	ydjU
Ordered Locus Names:	b1746, JW5282

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributesHide

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

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. Ref.6
Catalytic activity	N-succinyl-L-glutamate 5-semialdehyde + NAD+ + H2O = N-succinyl-L-glutamate + NADH. HAMAP MF_01174
Pathway	Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 4/5. Ref.4
Induction	By nitrogen starvation, and arginine. Induced at stationary phase by sigma S. Ref.4 Ref.5
Sequence similarities	Belongs to the aldehyde dehydrogenase family. AstD subfamily.
Biophysicochemical properties	Kinetic parameters: KM=91 µM for decanal Ref.6 KM=160 µM for NAD (at pH 8.5) KM=1.72 mM for succinic semialdehyde (at pH 8.5) Vmax=5.0 µmol/min/mg enzyme with decanal as substrate Vmax=0.69 µmol/min/mg enzyme with succinic semialdehyde as substrate

OntologiesHide

Keywords
Biological process	Arginine metabolism Stress response
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine catabolic process to glutamate Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction. Source: IntAct succinylglutamate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactionsHide

With	Entry	#Exp.	IntAct	Notes
mutH	P06722	1	EBI-545161,EBI-545170

Sequence annotation (Features)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 492	492	N-succinylglutamate 5-semialdehyde dehydrogenase HAMAP MF_01174		PRO_0000056569
Regions
	Nucleotide binding	220 – 225	6	NAD By similarity
Sites
	Active site	243	1	By similarity
	Active site	277	1	By similarity

SequencesHide

	Sequence		Length	Mass (Da)
	P76217-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: CA01ACE48D9CA8DB	FASTA	492	53,026
	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

ReferencesHide

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." 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. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli." Schneider B.L., Kiupakis A.K., Reitzer L.J. J. Bacteriol. 180:4278-4286(1998) [PubMed: 9696779] [Abstract] Cited for: INDUCTION, PATHWAY.
[5]	"ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli." Kiupakis A.K., Reitzer L. J. Bacteriol. 184:2940-2950(2002) [PubMed: 12003934] [Abstract] Cited for: INDUCTION.
[6]	"Enzyme genomics: application of general enzymatic screens to discover new enzymes." Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F. FEMS Microbiol. Rev. 29:263-279(2005) [PubMed: 15808744] [Abstract] Cited for: FUNCTION, KINETIC PARAMETERS.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC74816.1. AP009048 Genomic DNA. Translation: BAA15538.2.
PIR	B64934.
RefSeq	AP_002365.1. NP_416260.1.
3D structure databases
SMR	P76217. Positions 3-458.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9186N.
IntAct	P76217. 1 interaction.
STRING	P76217.
Genome annotation databases
EnsemblBacteria	EBESCT00000004367; EBESCP00000004367; EBESCG00000003561. EBESCT00000004368; EBESCP00000004368; EBESCG00000003561. EBESCT00000004369; EBESCP00000004369; EBESCG00000003561. EBESCT00000018380; EBESCP00000017671; EBESCG00000017434.
GeneID	946260.
GenomeReviews	Gene locus JW5282 in contig AP009048_GR. Gene locus b1746 in contig U00096_GR.
KEGG	ecj:JW5282. eco:b1746.
Organism-specific databases
EchoBASE	EB3753.
EcoGene	EG13997. astD.
CMR	Search...
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HBG752218.
OMA	KAYHART.
ProtClustDB	PRK09457.
Enzyme and pathway databases
BioCyc	EcoCyc:SUCCGLUALDDEHYD-MONOMER. ECOL168927:B1746-MONOMER. MetaCyc:SUCCGLUALDDEHYD-MONOMER.
BRENDA	1.2.1.3. 246.
Gene expression databases
Genevestigator	P76217.
Family and domain databases
HAMAP	MF_01174. Aldedh_AstD. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR017649. SuccinylGlu_semiald_DH_AstD. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR03240. arg_catab_astD. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry informationHide

Entry name

ASTD_ECOLI

Accession

Primary (citable) accession number: P76217
Secondary accession number(s): P78169, P78170

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	February 1, 1997
Last modified:	June 15, 2010
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)