 |
|
| PROSITE documentation PDOC00643 |
Alpha-isopropylmalate and homocitrate synthases signatures
Description
The following enzymes have been shown [1] to be functionally as well as
evolutionary related:
- α-isopropylmalate synthase (EC 2.3.3.13) which catalyzes the first step
in the biosynthesis of leucine, the condensation of acetyl-CoA and α-
ketoisovalerate to form 2-isopropylmalate synthase.
- Homocitrate synthase (EC 2.3.3.14) (gene nifV) which is involved in the
biosynthesis of the iron-molybdenum cofactor of nitrogenase and catalyzes
the condensation of acetyl-CoA and α-ketoglutarate into homocitrate.
- Soybean late nodulin 56.
- Methanococcus jannaschii hypothetical proteins MJ0503, MJ1195 and MJ1392.
We have selected two conserved regions as signature patterns for these
enzymes. The first region is located in the N-terminal section while the
second region is located in the central section and contains two conserved
histidine residues which could be implicated in the catalytic mechanism.
April 2006 / Pattern revised.
Technical section
PROSITE methods (with tools and information) covered by this documentation:
| AIPM_HOMOCIT_SYNTH_1, PS00815; Alpha-isopropylmalate and homocitrate synthases signature 1 (PATTERN) |
| Consensus pattern: |
L-R-[DE]-G-x-Q-x(4)-{L}-x(5)-K
|
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1SR9 2ZTJ 2ZTK 2ZYF ... [ALL] |
| AIPM_HOMOCIT_SYNTH_2, PS00816; Alpha-isopropylmalate and homocitrate synthases signature 2 (PATTERN) |
| Consensus pattern: |
[LIVMFW]-x(2)-H-x-H-[DN]-D-x-G-x-[GAS]-x-[GASLI]
|
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1SR9 2ZTJ 2ZTK 2ZYF ... [ALL] |
Reference
| 1 |
Authors |
Wang S.-Z., Dean D.R., Chen J.S., Johnson J.L. |
| Title |
The N-terminal and C-terminal portions of NifV are encoded by two different genes in Clostridium pasteurianum. |
| Source |
J. Bacteriol. 173:3041-3046(1991). |
| PubMed ID |
2022611 |
Copyright
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
Prosite License
or
see:
prosite_license.html.
Miscellaneous
View entry in original PROSITE document format
View entry in raw text format (no links)