argI:Gene Product(s)
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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 |
ArgI product |
|---|---|
| Synonyms |
ornithine carbamoyltransferase 1 product[1], B4254 product[2][1], ArgI product[2][1] |
| Product description |
Component of ; ornithine carbamoyltransferase[2][3] |
| EC number (for enzymes) | |
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Notes
Function
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 |
F |
Table 4 shows specific activity of ornithine transcarbamylase in argI. |
required field missing | ||||
| GO:0004585 |
ornithine carbamoyltransferase activity |
F |
Activity of enzyme presented in Fig. 3. Table 1 displays quantification of enzyme protocol. |
required field missing | ||||
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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
Physical Properties
| Sequence |
MSGFYHKHFL KLLDFTPAEL NSLLQLAAKL KADKKSGKEE AKLTGKNIAL IFEKDSTRTR CSFEVAAYDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGYG QEIVETLAEY ASVPVWNGLT NEFHPTQLLA DLLTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT GLDLRLVAPQ ACWPEAALVT ECRALAQQNG GNITLTEDVA KGVEGADFIY TDVWVSMGEA KEKWAERIAL LREYQVNSKM MQLTGNPEVK FLHCLPAFHD DQTTLGKKMA EEFGLHGGME VTDEVFESAA SIVFDQAENR MHTIKAVMVA TLSK |
|---|---|
| Mol. Wt |
36.91 kDa (calc) [2] |
| pI |
6.24[2] |
| Extinction coefficient |
36900 - 37400 (calc based on 10 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 |
|---|---|---|---|---|
|
X-RAY DIFFRACTION |
Escherichia coli |
2OTC ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH N-(PHOSPHONACETYL)-L-ORNITHINE |
||
|
X-RAY DIFFRACTION |
Escherichia coli |
1DUV CRYSTAL STRUCTURE OF E. COLI ORNITHINE TRANSCARBAMOYLASE COMPLEXED WITH NDELTA-L-ORNITHINE-DIAMINOPHOSPHINYL-N-SULPHONIC ACID (PSORN) |
||
|
X-RAY DIFFRACTION |
Escherichia coli |
1AKM ORNITHINE TRANSCARBAMYLASE FROM ESCHERICHIA COLI |
||
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Notes
Gene Product Resources
| Resource type | Source | Notes/Reference |
|---|---|---|
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Notes
Accessions in Other Databases
| Database | Accession | Notes |
|---|---|---|
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Notes
Links
| Name | URL | Comments |
|---|---|---|
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 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)
- ↑ 2.0 2.1 2.2 2.3 2.4 2.5 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 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
- ↑ Glansdorff, N et al. () The dual genetic control of ornithine transcarbamylase synthesis in Escherichia coli K12. Mutat. Res. 4 743-51 PubMed
- ↑ 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
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