NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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

CP000117; ABA20056.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_320951.1; -.

3D structure databases

ModBase

Q3MG30.

Enzyme and pathway databases

BioCyc

AVAR240292:AVA_0430-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: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.

PS01224; ARGC; 1.

Genome annotation databases

GeneID

3682591; -.

GenomeReviews

CP000117_GR; Ava_0430.

KEGG

ava:Ava_0430; -.

NMPDR

fig|240292.3.peg.1312; -.

Phylogenomic databases

HOGENOM

Q3MG30; -.

Genome annotation databases

CMR

Q3MG30; Ava_0430.

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`	`1 322`	`322`	`N-acetyl-gamma-glutamyl-phosphate reductase.`	`PRO_1000065137`
`ACT_SITE`	`117 117`		`By similarity.`

Sequence information

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

Molecular weight: 34832 Da [This is the MW of the unprocessed precursor]

CRC64: A01B081ADD12A23C [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 VHSSQVKILD ASTAYRTAQG WVYGFPELNP 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 ASFKDPSLLR DGTFLDATAV NGTNIVQVFV FANDNTKEAL LVARLDNLGK 

       310        320 
GASGAAVQNL NIMLGLPEEL GL

Q3MG30 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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