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PEC Original Annotations
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Essentiality
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Class
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non-essential
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References (PMID)
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Deletion
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16-1-2
(LD)
,
DE(sbcB-rfb)202
,
OCL74-2,75-5 (LD 16-1-2_CRS)
(D)
,
OCL74-2,75-6 (LD 16-1-2_P/O)
(D)
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Related gene (W3110 PEC)
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Gene Search
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Search MG1655 PEC by gene name:
hisG
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Related strains
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Strains Search
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Search strains by gene name:
hisG
Search strains by all related name:
hisG b2019 ECK2014 JW2001
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General information (Go to Linear View: )
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Gene Name
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hisG
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Alternative name
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b2019,ECK2014,JW2001
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Location, Length
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2,088,216 - 2,089,115
(
+
)
;
45.01
min
;
900
(bp) ,
299
(aa)
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Product
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ATP phosphoribosyltransferase
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Operon Name
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hisLGDCBHAFI
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Note
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GO_component: GO:0005737 - cytoplasm; GO_process: GO:0000105 - histidine biosynthetic process
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Function
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enzyme; Amino acid biosynthesis: Histidine
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Gene Ontology
|
GO:0000105
;
histidine biosynthetic process ( hisG )
GO:0000287
;
magnesium ion binding ( hisG )
GO:0003879
;
ATP phosphoribosyltransferase activity ( hisG )
GO:0005737
;
cytoplasm ( hisG )
GO:0008652
;
amino acid biosynthetic process ( hisG )
GO:0016740
;
transferase activity ( hisG )
GO:0016757
;
transferase activity, transferring glycosyl groups ( hisG )
GO:0046872
;
metal ion binding ( hisG )
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PID
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1788330
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EC number
(KEGG Pathway)
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2.4.2.17
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SWISS-PROT
(
Show simple
)
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Entry name(Acc.no)
|
HIS1_ECOLI
(
P60757
;
P10366
)
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- Protein name
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ATP phosphoribosyltransferase
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- Synonyms
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EC 2.4.2.17, ATP-PRTase, ATP-PRT
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- Gene name
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Name=hisG; OrderedLocusNames=b2019;
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- Comments
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FUNCTION:Catalyzes the condensation of ATP and PRPP to form N'-5'-phosphoribosyl-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of hisG enzymatic activity.
CATALYTIC ACTIVITY:1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
COFACTOR:Magnesium (Probable).
ENZYME REGULATION:Feedback inhibited by histidine. Also inhibited by AMP and PR-ATP.
PATHWAY:Histidine biosynthesis; first step.
SUBUNIT:Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme.
SUBCELLULAR LOCATION:Cytoplasmic.
SIMILARITY:Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
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Entry name(Acc.no)
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HIS1_ECOL6
(
P60758
;
P10366
)
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- Protein name
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ATP phosphoribosyltransferase
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- Synonyms
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EC 2.4.2.17, ATP-PRTase, ATP-PRT
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- Gene name
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Name=hisG; OrderedLocusNames=c2546;
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- Comments
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FUNCTION:Catalyzes the condensation of ATP and PRPP to form N'-5'-phosphoribosyl-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of hisG enzymatic activity (By similarity).
CATALYTIC ACTIVITY:1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
COFACTOR:Magnesium (By similarity).
ENZYME REGULATION:Feedback inhibited by histidine (By similarity).
PATHWAY:Histidine biosynthesis; first step.
SUBUNIT:Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme (By similarity).
SUBCELLULAR LOCATION:Cytoplasmic (By similarity).
SIMILARITY:Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
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Entry name(Acc.no)
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HIS1_ECO57
(
Q8X8T4
;
Q9WX46
)
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- Protein name
|
ATP phosphoribosyltransferase
|
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- Synonyms
|
EC 2.4.2.17, ATP-PRTase, ATP-PRT
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- Gene name
|
Name=hisG; OrderedLocusNames=z3181, ECs2820;
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- Comments
|
FUNCTION:Catalyzes the condensation of ATP and PRPP to form N'-5'-phosphoribosyl-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of hisG enzymatic activity (By similarity).
CATALYTIC ACTIVITY:1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate.
COFACTOR:Magnesium (By similarity).
ENZYME REGULATION:Feedback inhibited by histidine (By similarity).
PATHWAY:Histidine biosynthesis; first step.
SUBUNIT:Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme (By similarity).
SUBCELLULAR LOCATION:Cytoplasmic (By similarity).
SIMILARITY:Belongs to the ATP phosphoribosyltransferase family. Long subfamily.
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MMBR References
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Proc Natl Acad Sci U S A. 1981;78:2767-2771
In vivo and in vitro detection of the leader RNA of the histidine operon of Escherichia coli K-12.
Frunzio, R., C. B. Bruni, and F. Blasi.
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J Biol Chem. 1961;236:2261-7.
Interference with the feed-back control of histidine biosynthesis.
Moyed HS.
(
13773370
)
|
Nucleic Acids Res. 1981;9:2075-2086
Identification, nucleotide sequence and expression of the regulatory region of the histidine operon of Escherichia coli K-12.
Verde, P., R. Frunzio, P. P. di Nocera, F. Blasi, and C. B. Bruni.
|
J Bacteriol. 1980;142(1):32-42.
Structural and physiological studies of the Escherichia coli histidine operon inserted into plasmid vectors.
Bruni CB, Musti AM, Frunzio R, Blasi F.
(
6246067
)
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| Sequences |
Amino acid
FASTA format
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0001 MTDNTRLRIA MQKSGRLSDD SRELLARCGI KINLHTQRLI AMAENMPIDI LRVRDDDIPG LVMDGVVDLG
0071 IIGENVLEEE LLNRRAQGED PRYFTLRRLD FGGCRLSLAT PVDEAWDGPL SLNGKRIATS YPHLLKRYLD
0141 QKGISFKSCL LNGSVEVAPR AGLADAICDL VSTGATLEAN GLREVEVIYR SKACLIQRDG EMEESKQQLI
0211 DKLLTRIQGV IQARESKYIM MHAPTERLDE VIALLPGAER PTILPLAGDQ QRVAMHMVSS ETLFWETMEK
0281 LKALGASSIL VLPIEKMME
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Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 TGCATGAACG CATGAGAAAG CCCCCGGAAG
-070 ATCACCTTCC GGGGGCTTTT TTATTGCGCG GTTGATAACG GTTCAGACAG GTTTAAAGAG GAATAACAAA
0001 atgacagaca acactcgttt acgcatagct atgcagaaat ccggccgttt aagtgatgac tcacgcgaat
0071 tgctggcgcg ctgtggcatt aaaattaatc ttcacaccca gcgcctgatc gcgatggcag aaaacatgcc
0141 gattgatatt ctgcgcgtgc gtgacgacga cattcccggt ctggtaatgg atggcgtggt agaccttggg
0211 attatcggcg aaaacgtgct ggaagaagag ctgcttaacc gccgcgccca gggtgaagat ccacgctact
0281 ttaccctgcg tcgtctggat ttcggcggct gtcgtctttc gctggcaacg ccggttgatg aagcctggga
0351 cggtccgctc tccttaaacg gtaaacgtat cgccacctct tatcctcacc tgctcaagcg ttatctcgac
0421 cagaaaggca tctcttttaa atcctgctta ctgaacggtt ctgttgaagt cgccccgcgt gccggactgg
0491 cggatgcgat ttgcgatctg gtttccaccg gtgccacgct ggaagctaac ggcctgcgcg aagtcgaagt
0561 tatctatcgc tcgaaagcct gcctgattca acgcgatggc gaaatggaag aatccaaaca gcaactgatc
0631 gacaaactgc tgacccgtat tcagggtgtg atccaggcgc gcgaatcaaa atacatcatg atgcacgcac
0701 cgaccgaacg tctggatgaa gtcatcgccc tgctgccagg tgccgaacgc ccaactattc tgccgctggc
0771 gggtgaccaa cagcgcgtag cgatgcacat ggtcagcagc gaaaccctgt tctgggaaac catggaaaaa
0841 ctgaaagcgc tgggtgccag ttcaattctg gtcctgccga ttgagaagat gatggagtga TCGCCATGAG
0911 CTTTAACACA ATCATTGACT GGAATAGCTG TACTGCGGAG CAACAACGCC AGCTGTTAAT GCGCCCGGCG
0981 ATTTCCGCCT CTGAAAGCAT
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