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UniProtKB/Swiss-Prot entry O50146

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information

Entry name

ARGC2_THET2

Primary accession number

O50146

Secondary accession number

Q9ZND6

Integrated into Swiss-Prot on

December 1, 2000

Sequence was last modified on

December 1, 2000 (Sequence version 2)

Annotations were last modified on

November 25, 2008 (Entry version 65)

Name and origin of the protein

Protein name

N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase

Synonyms

AGPR
EC 1.2.1.38
EC 1.2.1.-
N-acetyl-glutamate semialdehyde/N-acetyl-aminoadipate semialdehyde dehydrogenase
NAGSA dehydrogenase

Gene name

	Name:	argC2
	Synonyms:	argC, lysY
	OrderedLocusNames:	TT_C1542

From

Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)

[TaxID: 262724]

[HAMAP proteome]

Taxonomy

Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nbt956; PubMed=15064768 [NCBI, ExPASy, EBI, Israel, Japan] Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; "The genome sequence of the extreme thermophile Thermus thermophilus."; Nat. Biotechnol. 22:547-553(2004).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236. PubMed=10074061 [NCBI, ExPASy, EBI, Israel, Japan] Kobashi N., Nishiyama M., Tanokura M.; "Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: lysine is synthesized via alpha-aminoadipic acid not via diaminopimelic acid."; J. Bacteriol. 181:1713-1718(1999).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-344. DOI=10.1016/S0378-1097(97)00456-4; PubMed=9418242 [NCBI, ExPASy, EBI, Israel, Japan] Kosuge T., Hoshino T.; "Molecular cloning and sequence analysis of the lysR gene from the extremely thermophilic eubacterium, Thermus thermophilus HB27."; FEMS Microbiol. Lett. 157:73-79(1997).

Comments

FUNCTION: Involved in both the arginine and lysine biosynthetic pathways (By similarity).
CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP⁺ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
CATALYTIC ACTIVITY: N²-acetyl-L-aminoadipate-semialdehyde + NADP⁺ + phosphate = N²-acetyl-L-gamma-aminoadipyl phosphate + NADPH.
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4 .
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 3/5 .
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

AE017221; AAS81884.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB017109; BAA74767.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006681; BAA23878.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T43947; T43947.

RefSeq

YP_005511.1; -.

3D structure databases

ModBase

O50146.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-6802; -.
TTHE262724:TT_C1542-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:0009085;	Biological process: lysine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
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

GeneID

2776302; -.

GenomeReviews

AE017221_GR; TT_C1542.

Phylogenomic databases

HOGENOM

O50146; -.

Genome annotation databases

CMR

O50146; TT_C1542.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 344`	`344`	`N-acetyl-gamma-glutamyl-phosphate/N-acetyl-gamma-aminoadipyl-phosphate reductase.`	`PRO_0000112501`
`ACT_SITE`	`148 148`		`By similarity.`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 38051 Da [This is the MW of the unprocessed precursor]

CRC64: B11CE66CB2F04C15 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDKKTLSIVG ASGYAGGEFL RLALSHPYLE VKQVTSRRFA GEPVHFVHPN LRGRTNLKFI 

        70         80         90        100        110        120 
PPEKLEPADI LVLALPHGVF AREFDRYSAL APILIDLSAD FRLKDPELYR RYYGEHPRPD 

       130        140        150        160        170        180 
LLGCFVYAVP ELYREALKGA DWIAGAGCNA TATLLGLYPL LKAGVLKPTP IFVTLLISTS 

       190        200        210        220        230        240 
AAGAEASPAS HHPERAGSIR VYKPTGHRHT AEVVENLPGR PEVHLTAIAT DRVRGILMTA 

       250        260        270        280        290        300 
QCFVQDGWSE RDVWQAYREA YAGEPFIRLV KQKKGVHRYP DPRFVQGTNY ADIGFELEED 

       310        320        330        340 
TGRLVVMTAI DNLVKGTAGH ALQALNVRMG WPETLGLDFP GLHP

O50146 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