argF:Gene Product(s): Difference between revisions

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!Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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[[Category:GO:0005737_!_cytoplasm]][[:Category:GO:0005737_!_cytoplasm|GO:0005737]]  
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cytoplasm  
cytoplasm  
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required fields missing   
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[[Category:GO:0006526_!_arginine_biosynthetic_process]][[:Category:GO:0006526_!_arginine_biosynthetic_process|GO:0006526]]  
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arginine biosynthetic process  
arginine biosynthetic process  
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[[Category:GO:0004585_!_ornithine_carbamoyltransferase_activity]][[:Category:GO:0004585_!_ornithine_carbamoyltransferase_activity|GO:0004585]]
[[Category:GO:0004585_!_ornithine_carbamoyltransferase_activity]][http://gowiki.tamu.edu/wiki/index.php/Category:GO:0004585_!_ornithine_carbamoyltransferase_activity GO:0004585]
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ornithine carbamoyltransferase activity
ornithine carbamoyltransferase activity
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complete  
complete  
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ornithine carbamoyltransferase activity
ornithine carbamoyltransferase activity
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complete  
complete  
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Revision as of 00:11, 29 July 2008

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

ArgF product

Synonyms

CP4-6 prophage; ornithine carbamoyltransferase 2, chain F product[1], B0273 product[2][1], ArgF product[2][1]

Product description

ArgF[2][3];

Component of ; ornithine carbamoyltransferase[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

C

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006526

arginine biosynthetic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0004585

ornithine carbamoyltransferase activity

PMID:4873401[4]

IGI: Inferred from Genetic Interaction

F

Table 4 shows specific activity of ornithine transcarbamylase in argF.

complete

GO:0004585

ornithine carbamoyltransferase activity

PMID:4558857[5]

IGI: Inferred from Genetic Interaction

F

Activity of enzyme presented in Fig. 3. Table 1 displays quantification of enzyme protocol.

complete

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Interactions

Partner Type Partner Notes

Protein

Subunits of ornithine carbamoyltransferase

could be indirect

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Notes

Localization

Compartment Description Evidence Notes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc 

MSDLYKKHFL KLLDFTPAQF TSLLTLAAQL KADKKNGKEV QKLTGKNIAL IFEKDSTRTR
CSFEVAAFDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGHG QEVVETLAQY
AGVPVWNGLT NEFHPTQLLA DLMTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT
GLDLRLLAPK ACWPEESLVA ECSALAEKHG GKITLTEDVA AGVKGADFIY TDVWVSMGEA
KEKWAERIAL LRGYQVNAQM MALTDNPNVK FLHCLPAFHD DQTTLGKQMA KEFDLHGGME
VTDEVFESAA SIVFDQAENR MHTIKAVMMA TLGE
Mol. Wt

36.83 kDa (calc) [2]

pI
Extinction coefficient

33920 - 34420 (calc based on 8 Y, 4 W, and 4 C residues)

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Domains/Motifs/Modification Sites

Type Residues Description Notes
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Structure

Structure Type Organism Accession Residues covered Notes
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Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:CHAINF-MONOMER

SwissModel (EcoliWiki Page)

SwissModel:P06960

UniProt (EcoliWiki Page)

UniProt:P06960

PFAM (EcoliWiki Page)

PFAM:PF02729

RefSeq (EcoliWiki Page)

RefSeq:NP_414807

ModBase (EcoliWiki Page)

ModBase:P06960

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Notes

Links

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Name URL Comments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ Glansdorff, N et al. () The dual genetic control of ornithine transcarbamylase synthesis in Escherichia coli K12. Mutat. Res. 4 743-51 PubMed
  5. ↑ Legrain, C et al. (1972) The dual genetic control of ornithine carbamolytransferase in Escherichia coli. A case of bacterial hybrid enzymes. Eur. J. Biochem. 27 93-102 PubMed


Categories

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