NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

Comments

FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate (By similarity).
CATALYTIC ACTIVITY: N-succinyl-L-glutamate 5-semialdehyde + NAD⁺ + H₂O = N-succinyl-L-glutamate + NADH.
PATHWAY: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 4/5 .
SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD subfamily.
SEQUENCE CAUTION:
- Sequence=AAN43073.1; Type=Frameshift; Positions=456;

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

AE005674; AAN43073.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP16966.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_707366.2; -.
NP_837159.1; -.

3D structure databases

ModBase

Q7UCI7.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN43073.1-MON; -.

Ontologies

GO:0019544;	Biological process: arginine catabolic process to glutamate (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

GeneID

1024647; -.
1077920; -.

GenomeReviews

AE014073_GR; S1597.
AE005674_GR; SF1479.1.

KEGG

sfx:S1597; -.

Phylogenomic databases

HOGENOM

Q7UCI7; -.

Genome annotation databases

CMR

Q7UCI7; SF1479.1.

Other

UniRef

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

Keywords

Arginine metabolism; Complete proteome; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 492`	`492`	`N-succinylglutamate 5-semialdehyde dehydrogenase.`	`PRO_0000262429`
`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: 53012 Da [This is the MW of the unprocessed precursor]

CRC64: 9A90CDE0C2A5AA00 [This is a checksum on the sequence]

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

        70         80         90        100        110        120 
RQVVVERFAG 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 GDAFLASLVA 

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

       370        380        390        400        410        420 
GIIEMTGVGG VPDEEVFGPF LRVWRYDTFD EAIRMANNTR FGLFCGLVSP EREKFDQLLL 

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

       490 
NPGLDFSDEV VR

Q7UCI7 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