MG1655
W3110
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Gene Report : argF
PEC Original Annotations
Essentiality
     Class non-essential
     References (PMID)
Microbiol Mol Biol Rev. 1998;62(3):814-984
Linkage map of Escherichia coli K-12, edition 10: the traditional map.
Berlyn MK. ( 9729611 )
     Deletion 9-1 (LD)  ,  DE(gpt-lac)5  ,  OCR36,37-6 (LD 9C::Ap) (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  argF
Related strains
     Strains Search Search strains by gene name:  argF   Search strains by all related name:  argF Arg5 argD b0273 ECK0274 JW0266

General information  (Go to Linear View:)
 Gene Name argF  
 Alternative name Arg5,argD,b0273,ECK0274,JW0266  
 Location, Length 288,525 - 289,529 (  -  ) ;   6.22 min ; 1005 (bp) ,   334 (aa) Go to Linear View
 Product ornithine carbamoyltransferase 2, chain F; CP4-6 prophage  
 Operon Name argF  
 Note ornithine carbamoyltransferase 2, chain F; GO_component: GO:0005737 - cytoplasm; GO_process: GO:0006526 - arginine biosynthetic process  
 Function enzyme; Amino acid biosynthesis: Arginine; Phage or Prophage Related  
 Gene Ontology GO:0003824; catalytic activity ( argD )
GO:0003992; acetylornithine transaminase activity ( argD )
GO:0004585; ornithine carbamoyltransferase activity ( argF )
GO:0005737; cytoplasm ( argD )
GO:0005737; cytoplasm ( argF )
GO:0006520; amino acid metabolic process ( argF )
GO:0006525; arginine metabolic process ( argD )
GO:0006526; arginine biosynthetic process ( argD )
GO:0006526; arginine biosynthetic process ( argF )
GO:0008483; transaminase activity ( argD )
GO:0008652; amino acid biosynthetic process ( argD )
GO:0008652; amino acid biosynthetic process ( argF )
GO:0009016; succinyldiaminopimelate transaminase activity ( argD )
GO:0009085; lysine biosynthetic process ( argD )
GO:0009348; ornithine carbamoyltransferase complex ( argF )
GO:0016597; amino acid binding ( argF )
GO:0016740; transferase activity ( argD )
GO:0016740; transferase activity ( argF )
GO:0016743; carboxyl- or carbamoyltransferase activity ( argF )
GO:0030170; pyridoxal phosphate binding ( argD )
 PID 1786469  
 EC number
  (KEGG Pathway)
 
2.1.3.3  
Verified Protein Starts (data compiled from literature and appropriate citations are available from EcoGene)
     EcoGene argF ( EG10067 )  
    Number of removed 1 aa cleaved  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) OTC2_ECOLI ( P06960 ; P78308 )
    -  Protein name Ornithine carbamoyltransferase chain F  
    -  Synonyms EC 2.1.3.3, OTCase-2  
    -  Gene name Name=argF; OrderedLocusNames=b0273;  
    -  Comments
  • CATALYTIC ACTIVITY:Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.
  • PATHWAY:Arginine biosynthesis; sixth step.
  • SUBUNIT:Trimer of identical or nonidentical chains, which are coded by two duplicated genes (argI and argF) at different loci.
  • SUBCELLULAR LOCATION:Cytoplasmic.
  • SIMILARITY:Belongs to the ATCase/OTCase family.  
  •   botton Entry name(Acc.no) ARGD_ECOLI ( P18335 )
        -  Protein name Acetylornithine/succinyldiaminopimelate aminotransferase  
        -  Synonyms EC 2.6.1.11, EC 2.6.1.17, ACOAT, Succinyldiaminopimelate transferase, DapATase  
        -  Gene name Name=argD; Synonyms=dapC, dtu; OrderedLocusNames=b3359;  
        -  Comments
  • FUNCTION:Involved in both the arginine and lysine biosynthetic pathways.
  • CATALYTIC ACTIVITY:N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
  • CATALYTIC ACTIVITY:N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate.
  • COFACTOR:Pyridoxal phosphate.
  • PATHWAY:Arginine biosynthesis; fourth step.
  • PATHWAY:Lysine biosynthesis; diaminopimelate pathway; fourth step.
  • SUBCELLULAR LOCATION:Cytoplasmic (Probable).
  • MISCELLANEOUS:The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine.
  • SIMILARITY:Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.  
  •   botton Entry name(Acc.no) ARGD_ECOL6 ( P59317 )
        -  Protein name Acetylornithine/succinyldiaminopimelate aminotransferase  
        -  Synonyms EC 2.6.1.11, EC 2.6.1.17, ACOAT, Succinyldiaminopimelate transferase, DapATase  
        -  Gene name Name=argD; Synonyms=dapC; OrderedLocusNames=c4134;  
        -  Comments
  • FUNCTION:Involved in both the arginine and lysine biosynthetic pathways (By similarity).
  • CATALYTIC ACTIVITY:N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
  • CATALYTIC ACTIVITY:N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate.
  • COFACTOR:Pyridoxal phosphate (By similarity).
  • PATHWAY:Arginine biosynthesis; fourth step.
  • PATHWAY:Lysine biosynthesis; diaminopimelate pathway; fourth step.
  • SUBCELLULAR LOCATION:Cytoplasmic (Probable).
  • MISCELLANEOUS:The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine (By similarity).
  • SIMILARITY:Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.  
  •   botton Entry name(Acc.no) ARGD_ECO57 ( Q8X4S6 )
        -  Protein name Acetylornithine/succinyldiaminopimelate aminotransferase  
        -  Synonyms EC 2.6.1.11, EC 2.6.1.17, ACOAT, Succinyldiaminopimelate transferase, DapATase  
        -  Gene name Name=argD; Synonyms=dapC; OrderedLocusNames=z4720, ECs4210;  
        -  Comments
  • FUNCTION:Involved in both the arginine and lysine biosynthetic pathways (By similarity).
  • CATALYTIC ACTIVITY:N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
  • CATALYTIC ACTIVITY:N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate.
  • COFACTOR:Pyridoxal phosphate (By similarity).
  • PATHWAY:Arginine biosynthesis; fourth step.
  • PATHWAY:Lysine biosynthesis; diaminopimelate pathway; fourth step.
  • SUBCELLULAR LOCATION:Cytoplasmic (Probable).
  • MISCELLANEOUS:The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine (By similarity).
  • SIMILARITY:Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.  

  •  Linear View (Whole Mode)
    View Location
       280.0  –  305.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP argF (  homologous genes of other bacterias  )   argD (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, Ornithine Transcarbamylase From Escherichia Coli  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Ornithine carbamoyltransferase chain F  
             PSI-BLAST Ornithine carbamoyltransferase
        nr     (database updated : 2007.02.20 )
             BLAST CP4-6 prophage; ornithine carbamoyltransferase 2, chain F [Escherichia coli K12]  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    TYR_PHOSPHO_SITE    MYRISTYL    CARBAMOYLTRANSFERASE     

    Other Cross-Reference
        COG COG0078E 
        EcoCyc argF 

    MMBR References
    Gene. 1983;22(2-3):281-7.
    A partial restriction map of the proA-purE region of the Escherichia coli K12 chromosome.
    Hadley RG, Hu M, Timmons M, Yun K, Deonier RC. ( 6307829 )
    J Bacteriol. 1992;174(11):3836-7.
    Physical map location of the argFGH operon of Escherichia coli.
    Hendrickson W, Rudd KE. ( 1592837 )
    Mol Gen Genet. 1981;181(2):222-9.
    Mapping of IS1 elements flanking the argF gene region on the Escherichia coli K-12 chromosome.
    Hu M, Deonier RC. ( 6268939 )
    Mol Gen Genet. 1985;201(2):347-50.
    Amplification of the ArgF region in strain HfrP4X of E. coli K-12.
    Jessop AP, Clugston C. ( 3003538 )
    Eur J Biochem. 1972;27(1):93-102.
    The dual genetic control of ornithine carbamolytransferase in Escherichia coli. A case of bacterial hybrid enzymes.
    Legrain C, Halleux P, Stalon V, Glansdorff N. ( 4558857 )
    Gene. 1979;5(2):159-75.
    Mapping of restriction sites in the argF gene of Escherichia coli by partial endonuclease digestion of end-labeled DNA.
    Moore SK, James E. ( 376404 )
    Gene. 1981;16(1-3):119-32.
    Nucleotide sequence of the argF regulatory region of Escherichia coli K-12.
    Moore SK, Garvin RT, James E. ( 6282686 )
    EMBO J. 1982;1(7):853-7.
    Homologous control sites and DNA transcription starts in the related argF and argI genes of Escherichia coli K12.
    Piette J, Cunin R, Van Vliet F, Charlier D, Crabeel M, Ota Y, Glansdorff N. ( 6329710 )
    Nucleic Acids Res. 1984;12:6277-6289
    Evolutionary divergence of genes for ornithine and aspartate carbamoyl-transferase-complete sequence and mode of regulation of the Escherichia coli argF gene; comparison of argF with argI and pyrB.
    Van Vliet, F., R. Cunin, A. Jacobs, J. Piette, D. Gigot, M. Lauwereys, A. Pierard, and N. Glansdorff.
    Mol Gen Genet. 1981;181(2):230-40.
    Characterization of P1argF derivatives from Escherichia coli K12 transduction. I. IS1 elements flank the argF gene segment.
    York MK, Stodolsky M. ( 6268940 )
    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 MSDLYKKHFL KLLDFTPAQF TSLLTLAAQL KADKKNGKEV QKLTGKNIAL IFEKDSTRTR CSFEVAAFDQ 
    0071 GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGHG QEVVETLAQY AGVPVWNGLT NEFHPTQLLA 
    0141 DLMTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT GLDLRLLAPK ACWPEESLVA ECSALAEKHG 
    0211 GKITLTEDVA AGVKGADFIY TDVWVSMGEA KEKWAERIAL LRGYQVNAQM MALTDNPNVK FLHCLPAFHD 
    0281 DQTTLGKQMA KEFDLHGGME VTDEVFESAA SIVFDQAENR MHTIKAVMMA TLGE
    
    
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp
    -100                                             cctttgtaag aaagaattgt gaaatggggt 
    -070 tgcaaatgaa taattacaca tataaagtga attttaattc aataagtggc gttcgccatg cgaggataaa 
    0001 atgtccgatt tatacaaaaa acactttctg aaactgctcg actttacccc tgcacagttc acttctctgc 
    0071 tgacccttgc cgcacagctc aaagccgata aaaaaaatgg caaggaagta cagaagctta ccggtaaaaa 
    0141 catcgcgctc atcttcgaaa aagactcgac tcgtacccgt tgctctttcg aagttgccgc atttgaccag 
    0211 ggcgcgcgcg ttacctattt agggccgagc ggcagccaga ttgggcataa agagtcaatt aaggacaccg 
    0281 cgcgggttct cgggcggatg tatgacggca ttcagtatcg cggtcacggc caggaagtgg tcgaaacgct 
    0351 ggcgcagtat gcgggcgtgc cggtgtggaa cgggctgacc aacgagttcc acccgaccca gctgctggcg 
    0421 gacctgatga ccatgcagga gcacctgccg ggcaaggcgt ttaacgagat gacgctggtc tacgcgggcg 
    0491 atgcgcgcaa caacatgggc aactcgatgc tggaagcggc ggcgctgacc gggctggatc tgcgcctgtt 
    0561 ggccccgaaa gcctgctggc cggaagagag cctggtggcg gagtgcagcg cgctggcgga gaagcacggc 
    0631 gggaaaatta ctctgacgga agacgtggcg gcaggcgtta agggcgcgga ctttatctat accgacgtgt 
    0701 gggtgtcgat gggcgaggcc aaagagaagt gggcagagcg gattgcgctg ctgcgcgggt atcaggtgaa 
    0771 cgcgcagatg atggcgctga ccgacaaccc gaacgtgaag ttcctgcact gtctgccggc gttccatgac 
    0841 gaccagacta cgctcggcaa gcagatggcg aaggagttcg atctgcacgg cgggatggag gtgacggacg 
    0911 aggtgtttga gtcggcggcg agcatcgtgt tcgaccaggc ggaaaaccgg atgcatacga ttaaggcggt 
    0981 gatgatggca acgcttgggg agtgattggg tccgctgcgc gttggtgccc tcaccccggc cctctcccac 
    1051 agggagaggg agaacaccgg ctccatttca ttgatttttc atcccgaaaa aggta