Reviewed, UniProtKB/Swiss-Prot Q07906 (ARGC_BACST)

Names and origin

Protein names

Recommended name:
    N-acetyl-gamma-glutamyl-phosphate reductase
      Short name=AGPR
    EC=1.2.1.38
Alternative name(s):
    N-acetyl-glutamate semialdehyde dehydrogenase
      Short name=NAGSA dehydrogenase

Gene names

Name:

argC

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. HAMAP MF_00150
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4. HAMAP MF_00150
Subcellular location	Cytoplasm Probable HAMAP MF_00150.
Induction	Expression of the argCJBD operon is regulated by argR. This binding is arginine dependent. Ref.1
Sequence similarities	Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: HAMAP NAD or NADH binding Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 345	345	N-acetyl-gamma-glutamyl-phosphate reductase HAMAP MF_00150		PRO_0000112384
Sites
	Active site	149	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q07906-1 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: F488A7108E602FDD	FASTA	345	37,455
	10 20 30 40 50 60 MMNVAIIGAT GYSGAELFRL LYGHPHVSQC DVFSSSQDGI HLSESFPHVG AVDGAVLHKL 70 80 90 100 110 120 EIEALAKYDA VFFATPPGVS GEWAPALVDR GVKVIDLSGD FRLKDGAVYA QWYGREAAPS 130 140 150 160 170 180 AYLERAVYGL TEWNREAVRG AVLLSNPGCY PTATLLGLAP LVKEGLIKED SIIVDAKSGV 190 200 210 220 230 240 SGAGRKAGLG THFSEVNENV KIYKVNAHQH IPEIEQALQT WNEAVAPITF STHLIPMTRG 250 260 270 280 290 300 IMATIYAKAK QSISPNDLVD LYKTSYEGSP FVRIRQLGQF PATKDVYGSN YCDIGLAYDE 310 320 330 340 RTERVTVVSV IDNLMKGAAG QAVQNFNLMM GWDEAEGLRS LPIYP

References

[1]

"The arginine operon of Bacillus stearothermophilus: characterization of the control region and its interaction with the heterologous B. subtilis arginine repressor." Savchenko A., Charlier D.R.M., Dion M., Weigel P., Hallet J.-N., Holtham C., Baumberg S., Glansdorff N., Sakanyan V. Mol. Gen. Genet. 252:69-78(1996) [PubMed: 8804405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84, TRANSCRIPTIONAL REGULATION. Strain: NCIB 8224 / CCM 2186.

[2]

"Primary structure, partial purification and regulation of key enzymes of the acetyl cycle of arginine biosynthesis in Bacillus stearothermophilus: dual function of ornithine acetyltransferase." Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I., Pierard P., Glansdorff N. J. Gen. Microbiol. 139:393-402(1993) [PubMed: 8473852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-345. Strain: NCIB 8224 / CCM 2186.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06036 Genomic DNA. Translation: AAA22196.1.
PIR	S72490.
3D structure databases
SMR	Q07906. Positions 1-345.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.38. 266715.
Family and domain databases
HAMAP	MF_00150. ArgC_type1. [Tree]
InterPro	IPR000706. AGPR_act_site. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01850. argC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGC_BACST

Accession

Primary (citable) accession number: Q07906

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 4, 2005
Last modified:	February 9, 2010
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)