[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1111/j.1365-2958.1992.tb01381.x; PubMed=1406250 [NCBI, ExPASy, EBI, Israel, Japan] Floriano B., Herrero A., Flores E.; "Isolation of arginine auxotrophs, cloning by mutant complementation, and sequence analysis of the argC gene from the cyanobacterium Anabaena species PCC 7120."; Mol. Microbiol. 6:2085-2094(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=7929012 [NCBI, ExPASy, EBI, Israel, Japan] Floriano B., Herrero A., Flores E.; "Analysis of expression of the argC and argD genes in the cyanobacterium Anabaena sp. strain PCC 7120."; J. Bacteriol. 176:6397-6401(1994).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1093/dnares/8.5.205; PubMed=11759840 [NCBI, ExPASy, EBI, Israel, Japan] Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., Yasuda M., Tabata S.; "Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."; DNA Res. 8:205-213(2001).

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 2 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

X65511; CAA46483.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000019; BAB74197.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AC2118; AC2118.
S24753; S24753.

RefSeq

NP_486538.1; -.

3D structure databases

ModBase

P54894.

Enzyme and pathway databases

BioCyc

NSP103690:ALL2498-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: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_01110; -; 1.
PBIL [Tree]

InterPro

IPR000706; AGPR_act_site.
IPR010136; AGPR_subtype.
IPR000534; Semialdehyde_DHase_NAD-bd.
Graphical view of domain structure.

Pfam

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

ProDom

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

TIGRFAMs

TIGR01851; argC_other; 1.

PROSITE

PS01224; ARGC; 1.

Genome annotation databases

GeneID

1106095; -.

GenomeReviews

BA000019_GR; all2498.

KEGG

ana:all2498; -.

NMPDR

fig|103690.1.peg.2805; -.

Phylogenomic databases

HOGENOM

P54894; -.

Genome annotation databases

CMR

P54894; all2498.

Other

ProtoNet

P54894.

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`	`1 322`	`322`	`N-acetyl-gamma-glutamyl-phosphate reductase 2.`	`PRO_0000112503`
`ACT_SITE`	`117 117`		`By similarity.`

Sequence information

Length: 322 AA [This is the length of the unprocessed precursor]

Molecular weight: 34823 Da [This is the MW of the unprocessed precursor]

CRC64: 1C41BA71630942F0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNKPKIFIDG EAGTTGLQIY SRLNERDDIE LVSIAASKRK DADERAKLLN SVDVAILCLP 

        70         80         90        100        110        120 
DDAAREAVSL VNSSQVKILD ASTAYRTAQG WVYGFPEMNP GQREKIANAQ FVSNPGCYPT 

       130        140        150        160        170        180 
GFLACVRPLI AQGILPSSFP ITINAVSGYS GGGKSLIQKY DSFHEQQKGA TSDYPFGIYG 

       190        200        210        220        230        240 
LQFGHKHVKE MHQHSGLASP PLFIPAVGDF EQGMLVQIPL PLWTLDNPPS GEEIHQAIAQ 

       250        260        270        280        290        300 
YYQGEKFVQV APFKDPSLLR DGTFLDATAV NGTNIVQVFV FGNDNTKEAL LVARLDNLGK 

       310        320 
GASGAAVQNL NIMLGLPEEL GL

P54894 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