NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
DOI=10.1139/cjm-45-11-959; PubMed=10588044 [NCBI, ExPASy, EBI, Israel, Japan]
Hani E.K., Ng D., Chan V.-L.;
"Arginine biosynthesis in Campylobacter jejuni TGH9011: determination of the argCOBD cluster.";
Can. J. Microbiol. 45:959-969(1999).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).

Comments

CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP⁺ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4 .
INTERACTION:
Q0PAW9:flaG; NbExp=1; IntAct=EBI-1195272, EBI-1191365;
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1 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

AF093219; AAF21802.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL111168; CAL34379.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H81439; H81439.

3D structure databases

ModBase

Q9PIS0.

Protein-protein interaction databases

IntAct

Q9PIS0; -.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ0224-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003942;	Molecular function: N-acetyl-gamma-glutamyl-phosphate reductase activity (inferred from electronic annotation from HAMAP).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0046983;	Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0006526;	Biological process: arginine biosynthetic process (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_00150; -; 1.
PBIL [Tree]

InterPro

IPR000706; AGPR_act_site.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.

Pfam

PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.

ProDom

PD003765; AGPR_act_site; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01850; argC; 1.

PS01224; ARGC; 1.

Genome annotation databases

GenomeReviews

AL111168_GR; Cj0224.

KEGG

cje:Cj0224; -.

CMR

Q9PIS0; Cj0224.

Other

UniRef

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

Keywords

Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 342`	`342`	`N-acetyl-gamma-glutamyl-phosphate reductase.`	`PRO_0000112393`
`ACT_SITE`	`147 147`		`By similarity.`
`CONFLICT`	`76 76`		`K -> E (in Ref. 1; AAF21802).`
`CONFLICT`	`119 119`		`E -> D (in Ref. 1; AAF21802).`
`CONFLICT`	`168 168`		`S -> N (in Ref. 1; AAF21802).`
`CONFLICT`	`194 194`		`V -> I (in Ref. 1; AAF21802).`
`CONFLICT`	`202 202`		`N -> G (in Ref. 1; AAF21802).`
`CONFLICT`	`205 205`		`L -> S (in Ref. 1; AAF21802).`
`CONFLICT`	`296 296`		`V -> I (in Ref. 1; AAF21802).`

Sequence information

Length: 342 AA [This is the length of the unprocessed precursor]

Molecular weight: 38896 Da [This is the MW of the unprocessed precursor]

CRC64: D5CE90039C63179C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIKVGILGA SGYAGNELVR ILLNHPKVEI SYLGSSSSVG QNYQDLYPNT PLNLCFENKN 

        70         80         90        100        110        120 
LDELELDLLF LATPHKFSAK LLNENLLKKM KIIDLSADFR LKNPKDYELW YKFTHPNQEL 

       130        140        150        160        170        180 
LQNAVYGLCE LYKEEIKKAS LVANPGCYTT CSILSLYPLF KEKIIDFSSV IIDAKSGVSG 

       190        200        210        220        230        240 
AGRSAKVENL FCEVNENIKA YNLALHRHTP EIEEHLSYAA KEKITLQFTP HLVPMQRGIL 

       250        260        270        280        290        300 
ISAYANLKED LQEQDIRDIY TKYYQNNKFI RLLPPQSLPQ TRWVKSSNFA DINFSVDQRT 

       310        320        330        340 
KRVIVLGAID NLIKGAAGQA VQNMNLMFDF DEDEGLKFFA NL

Q9PIS0 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