NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376;
PubMed=9098069 [NCBI, ExPASy, EBI, Israel, Japan]
Bringel F., Frey L., Boivin S., Hubert J.-C.;
"Arginine biosynthesis and regulation in Lactobacillus plantarum: the carA gene and the argCJBDF cluster are divergently transcribed.";
J. Bacteriol. 179:2697-2706(1997).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
DOI=10.1073/pnas.0337704100; PubMed=12566566 [NCBI, ExPASy, EBI, Israel, Japan]
Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J.;
"Complete genome sequence of Lactobacillus plantarum WCFS1.";
Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).

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 .
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

X99978; CAA68239.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL935253; CAD63147.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_784306.1; -.

3D structure databases

ModBase

O08318.

Enzyme and pathway databases

BioCyc

LPLA220668:LP_0528-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]

TIGRFAMs

TIGR01850; argC; 1.

PROSITE

PS01224; ARGC; 1.

Genome annotation databases

GeneID

1061865; -.

GenomeReviews

AL935263_GR; lp_0528.

KEGG

lpl:lp_0528; -.

NMPDR

fig|220668.1.peg.440; -.

Phylogenomic databases

HOGENOM

O08318; -.

Genome annotation databases

CMR

O08318; lp_0528.

Other

ProtoNet

O08318.

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`	`1 341`	`341`	`N-acetyl-gamma-glutamyl-phosphate reductase 2.`	`PRO_0000112413`
`ACT_SITE`	`146 146`		`By similarity.`
`CONFLICT`	`119 119`		`S -> P (in Ref. 1; CAA68239).`
`CONFLICT`	`234 234`		`V -> A (in Ref. 1; CAA68239).`

Sequence information

Length: 341 AA [This is the length of the unprocessed precursor]

Molecular weight: 36940 Da [This is the MW of the unprocessed precursor]

CRC64: CD35D297041CC42A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQVALVGVTG YSGMVLYRLL KQHPEIDRIQ LYGHVGATTV ALKTVAAMYQ KETAVIRPFD 

        70         80         90        100        110        120 
ATAIMRDNAI VFFATSAGIT RQLALPFIAA HFPVIDLSGD FRLHDPEQYQ RWYQRDPASA 

       130        140        150        160        170        180 
TALAQASYGL ADMPAPLSTY IANPGCYATA TLLGLAPLAQ QQLVEPTSIV VDAKSGLSGA 

       190        200        210        220        230        240 
GKRATAASHY VAVNDNLSLY KLNQHQHIPE MMQQLQQWWS AISAIEFTTT LIPVTRGIMT 

       250        260        270        280        290        300 
TIYAKAKSAL TTTQVRAAFT ATYHEQPFVQ VLPTGMPTLK DVVGSNNCAL GVDYNPVTNT 

       310        320        330        340 
IVVVSVIDNL MKGAAGQAVQ NFNRYFDFAV TAGLPTLPVF P

O08318 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