|
PEC Original Annotations
|
|
Essentiality
|
|
Class
|
non-essential
|
|
References (PMID)
|
|
|
Deletion
|
OCR10
(D)
,
DE(ppc-argH)486
|
|
Related gene (W3110 PEC)
|
|
Gene Search
|
Search MG1655 PEC by gene name:
argC
|
|
Related strains
|
|
Strains Search
|
Search strains by gene name:
argC
Search strains by all related name:
argC Arg2 argH b3958 ECK3949 JW3930
|
General information (Go to Linear View: )
|
|
Gene Name
|
argC
|
|
Alternative name
|
Arg2,argH,b3958,ECK3949,JW3930
|
|
Location, Length
|
4,153,024 - 4,154,028
(
+
)
;
89.51
min
;
1005
(bp) ,
334
(aa)
|
|
Product
|
N-acetyl-gamma-glutamylphosphate reductase, NAD(P)-binding
|
|
Operon Name
|
argCBH
|
|
Note
|
N-acetyl-gamma-glutamylphosphate reductase; GO_component: GO:0005737 - cytoplasm; GO_process: GO:0006526 - arginine biosynthetic process
|
|
Function
|
enzyme; Amino acid biosynthesis: Arginine
|
|
Gene Ontology
|
GO:0003824
;
catalytic activity ( argC )
GO:0003824
;
catalytic activity ( argH )
GO:0003942
;
N-acetyl-gamma-glutamyl-phosphate reductase activity ( argC )
GO:0004056
;
argininosuccinate lyase activity ( argH )
GO:0005488
;
binding ( argC )
GO:0005737
;
cytoplasm ( argC )
GO:0005737
;
cytoplasm ( argH )
GO:0006520
;
amino acid metabolic process ( argC )
GO:0006526
;
arginine biosynthetic process ( argC )
GO:0006526
;
arginine biosynthetic process ( argH )
GO:0008152
;
metabolic process ( argC )
GO:0008652
;
amino acid biosynthetic process ( argC )
GO:0008652
;
amino acid biosynthetic process ( argH )
GO:0016491
;
oxidoreductase activity ( argC )
GO:0016620
;
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor ( argC )
GO:0016829
;
lyase activity ( argH )
GO:0042450
;
arginine biosynthetic process via ornithine ( argH )
GO:0046983
;
protein dimerization activity ( argC )
GO:0051287
;
NAD binding ( argC )
|
|
PID
|
1790396
|
EC number
(KEGG Pathway)
|
1.2.1.38
|
|
SWISS-PROT
(
Show simple
)
|
Entry name(Acc.no)
|
ARGC_ECOLI
(
P11446
)
|
|
- Protein name
|
N-acetyl-gamma-glutamyl-phosphate reductase
|
|
- Synonyms
|
EC 1.2.1.38, AGPR, N- acetyl-glutamate semialdehyde dehydrogenase, NAGSA dehydrogenase
|
|
- Gene name
|
Name=argC; OrderedLocusNames=b3958;
|
|
- Comments
|
CATALYTIC ACTIVITY:N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
PATHWAY:Arginine biosynthesis; third step.
SUBCELLULAR LOCATION:Cytoplasmic (Probable).
SIMILARITY:Belongs to the NAGSA dehydrogenase family. Subfamily 1.
|
|
Entry name(Acc.no)
|
ARGC_ECOL6
(
P59306
)
|
|
- Protein name
|
N-acetyl-gamma-glutamyl-phosphate reductase
|
|
- Synonyms
|
EC 1.2.1.38, AGPR, N- acetyl-glutamate semialdehyde dehydrogenase, NAGSA dehydrogenase
|
|
- Gene name
|
Name=argC; OrderedLocusNames=c4917;
|
|
- Comments
|
CATALYTIC ACTIVITY:N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
PATHWAY:Arginine biosynthesis; third step.
SUBCELLULAR LOCATION:Cytoplasmic (Probable).
SIMILARITY:Belongs to the NAGSA dehydrogenase family. Subfamily 1.
|
|
Entry name(Acc.no)
|
ARGC_ECO57
(
Q8X732
)
|
|
- Protein name
|
N-acetyl-gamma-glutamyl-phosphate reductase
|
|
- Synonyms
|
EC 1.2.1.38, AGPR, N- acetyl-glutamate semialdehyde dehydrogenase, NAGSA dehydrogenase
|
|
- Gene name
|
Name=argC; OrderedLocusNames=z5516, ECs4887;
|
|
- Comments
|
CATALYTIC ACTIVITY:N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
PATHWAY:Arginine biosynthesis; third step.
SUBCELLULAR LOCATION:Cytoplasmic (Probable).
SIMILARITY:Belongs to the NAGSA dehydrogenase family. Subfamily 1.
|
|
MMBR References
|
In K. D. MacDonald (ed.), Proceedings of the Second International Symposium on Genetics and Industrial Microorganisms. Academic Press, London, United Kingdom. 1976:369-389
Genetic control of arginine metabolism in prokaryotes.
Baumberg, S.
|
Gene. 1979;8(1):25-34.
Clustered arg genes on a BamHI segment of the Escherichia coli chromosome.
Moran MC, Mazaitis AJ, Vogel RH, Vogel HJ.
(
231541
)
|
J Bacteriol. 1982;151(1):62-7.
Promoter mapping and selection of operator mutants by using insertion of bacteriophage Mu in the argECBH divergent operon of Escherichia coli K-12.
Beny G, Boyen A, Charlier D, Lissens W, Feller A, Glansdorff N.
(
6211434
)
|
Gene. 1988;68(2):275-83.
Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes.
Parsot C, Boyen A, Cohen GN, Glansdorff N.
(
2851495
)
|
Nucleic Acids Res. 1982;10:8031-8048
The regulatory region of the divergent argECBH operon in Escherichia coli K-12.
Piette, J., R. Cunin, A. Boyen, D. Charlier, M. Crabeel, F. Van Vliet, N. Glansdorff, C. Squires, and C. L. Squires.
|
J Bacteriol. 1975;123(3):898-904.
Accumulation of arginine precursors in Escherichia coli: effects on growth, enzyme repression, and application to the forward selection of arginine auxotrophs.
Crabeel M, Charlier D, Cunin R, Boyen A, Glansdorff N, Pierard A.
(
1099083
)
|
Gene. 1979;5(3):207-31.
Cloning and endonuclease restriction analysis of argF and of the control region of the argECBH bipolar operon in Escherichia coli.
Crabeel M, Charlier D, Cunin R, Glansdorff N.
(
381103
)
|
| Sequences |
Amino acid
FASTA format
|
0001 MLNTLIVGAS GYAGAELVTY VNRHPHMNIT ALTVSAQSND AGKLISDLHP QLKGIVDLPL QPMSDISEFS
0071 PGVDVVFLAT AHEVSHDLAP QFLEAGCVVF DLSGAFRVND ATFYEKYYGF THQYPELLEQ AAYGLAEWCG
0141 NKLKEANLIA VPGCYPTAAQ LALKPLIDAD LLDLNQWPVI NATSGVSGAG RKAAISNSFC EVSLQPYGVF
0211 THRHQPEIAT HLGADVIFTP HLGNFPRGIL ETITCRLKSG VTQAQVAQVL QQAYAHKPLV RLYDKGVPAL
0281 KNVVGLPFCD IGFAVQGEHL IIVATEDNLL KGAAAQAVQC ANIRFGYAET QSLI
|
Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 TAAAAATACA CTAACGTTGA GCGTAATAAA
-070 ACCCACCAGC CGTAAGGTGA ATGTTTTACG TTTAACCTGG CAACCAGACA TAAGAAGGTG AATAGCCCCG
0001 atgttgaata cgctgattgt gggtgccagc ggctacgctg gcgcagagct agtgacctat gtaaatcgcc
0071 atccgcatat gaacataacc gctttgactg tttcagcgca aagcaatgat gcgggaaagt taatctccga
0141 tttgcatccg cagctaaaag gcatcgttga tctgccgttg cagccgatgt cggatatcag cgagtttagc
0211 ccaggggtgg acgtagtgtt tctcgccacc gcccatgaag ttagccacga tttagcgccg cagtttcttg
0281 aagcgggctg cgtggtgttc gacctttccg gcgcgtttcg tgttaacgac gccaccttct atgaaaaata
0351 ttacggcttt acccatcaat acccggaact gttggaacag gcagcctacg gtctggcgga gtggtgcggt
0421 aataaattaa aagaagcgaa tttgattgcg gtgccgggct gttatccgac ggcggcacag ctggcgctga
0491 aaccgttgat tgatgccgat cttcttgacc tcaatcagtg gccggtgatc aacgccacca gcggcgtgag
0561 cggtgcaggg cgtaaagcgg ccatttcaaa cagcttttgt gaagttagcc tgcaaccgta tggcgtcttt
0631 actcatcgcc atcaaccaga gatcgccaca cacctcggtg ctgacgttat cttcacccca catctgggca
0701 atttcccgcg cggcattctc gaaaccatta cctgccgcct gaaatcgggt gtgacccagg cgcaagtcgc
0771 gcaagtgtta cagcaggcgt atgcccataa accgctggtg cggctgtatg acaaaggcgt tccggcgctg
0841 aaaaatgtcg ttgggctgcc attttgcgat atcgggtttg ccgttcaggg cgagcatctg attattgtgg
0911 cgaccgaaga caacttactg aaaggcgcgg cggcacaagc ggtacagtgc gccaatattc gtttcggcta
0981 tgcggaaacg cagtctctta tttaaGGGTG CAATGATGAA TCCATTAATT ATCAAACTGG GCGGCGTACT
1051 GCTGGATAGT GAAGAGGCGC TGGAACGTCT GTTTAGCGCA CTGGTGAATT ATCGT
|
