NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
DOI=10.1073/pnas.0404172101; PubMed=15466707 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).

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

AP006841; BAD47281.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_097815.1; -.

3D structure databases

ModBase

Q64YZ5.

Enzyme and pathway databases

BioCyc

BFRA295405:BF0532-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

3082618; -.

AP006841_GR; BF0532.

bfr:BF0532; -.

fig|295405.3.peg.570; -.

Phylogenomic databases

HOGENOM

Q64YZ5; -.

Genome annotation databases

CMR

Q64YZ5; BF0532.

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_1000010978`
`ACT_SITE`	`132 132`		`By similarity.`

Sequence information

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

Molecular weight: 35937 Da [This is the MW of the unprocessed precursor]

CRC64: 19957F60E5ECB384 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIKAGIIGGA GYTAGELIRL LINHPETEIV FINSTSNAGN KITDVHEGLY GECDLTFTDE 

        70         80         90        100        110        120 
LPLEDIDVLF FCTAHGDTKK FMESHNIPEE LKIIDLSMDY RIASPDHDFI YGLPELNRRA 

       130        140        150        160        170        180 
TCTAKHVANP GCFATCIQLG LLPLAKHLML NEDVMVNAIT GSTGAGVKPG ATSHFSWRNN 

       190        200        210        220        230        240 
NMSVYKAFEH QHVPEIKQSL KQLQNSFDAE IDFIPYRGDF PRGIFATLVV KTKVALEEIV 

       250        260        270        280        290        300 
RMYEEYYAKD SFVHIVDKNI DLKQVVNTNK CLIHLEKHGD KLLIISCIDN LLKGASGQAV 

       310        320 
HNMNLMFNLE ETVGLRLKPS AF

Q64YZ5 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