| General information | | DisProt: | DP00398 | | Name: | Acetolactate synthase catalytic subunit, mitochondrial | | Synonym(s): | ILVB_YEAST
EC 2.2.1.6
Acetohydroxy-acid synthase catalytic subunit
ALS
AHAS
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P07342 | | UniGene: | | | SwissProt: | ILVB_YEAST | | TrEMBL: | | | NCBI (GI): | 124376 | | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | | Sequence length: | 687 | | Percent disordered: | 13% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MIRQSTLKNF AIKRCFQHIA YRNTPAMRSV ALAQRFYSSS SRYYSASPLP ASKRPEPAPS - 60
FNVDPLEQPA EPSKLAKKLR AEPDMDTSFV GLTGGQIFNE MMSRQNVDTV FGYPGGAILP - 120
VYDAIHNSDK FNFVLPKHEQ GAGHMAEGYA RASGKPGVVL VTSGPGATNV VTPMADAFAD - 180
GIPMVVFTGQ VPTSAIGTDA FQEADVVGIS RSCTKWNVMV KSVEELPLRI NEAFEIATSG - 240
RPGPVLVDLP KDVTAAILRN PIPTKTTLPS NALNQLTSRA QDEFVMQSIN KAADLINLAK - 300
KPVLYVGAGI LNHADGPRLL KELSDRAQIP VTTTLQGLGS FDQEDPKSLD MLGMHGCATA - 360
NLAVQNADLI IAVGARFDDR VTGNISKFAP EARRAAAEGR GGIIHFEVSP KNINKVVQTQ - 420
IAVEGDATTN LGKMMSKIFP VKERSEWFAQ INKWKKEYPY AYMEETPGSK IKPQTVIKKL - 480
SKVANDTGRH VIVTTGVGQH QMWAAQHWTW RNPHTFITSG GLGTMGYGLP AAIGAQVAKP - 540
ESLVIDIDGD ASFNMTLTEL SSAVQAGTPV KILILNNEEQ GMVTQWQSLF YEHRYSHTHQ - 600
LNPDFIKLAE AMGLKGLRVK KQEELDAKLK EFVSTKGPVL LEVEVDKKVP VLPMVAGGSG - 660
LDEFINFDPE VERQQTELRH KRTGGKH
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| Functional narrative |
Involved in amino acid biosynthesis.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 58 - 83 | | Length: | 26 | | Region sequence: |
APSFNVDPLEQPAEPSKLAKKLRAEP | | Modification type: | Complex
| | PDB: | 1JSC:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (FAD 1 mM; Mg2+ 1 mM; Potassium phosphate 0.2 M; ThDP 1 mM)
| References:
- Pang SS, Duggleby RG, Guddat LW. "Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors." J Mol Biol. 2002; 317(2): 249-62. PubMed: 11902841
| Comments:The mature protein, consisting of residues 58-687, was used for crystal structure determination. A 47 residue N-terminal peptide containing a hexahistidine tag was added.
This region was disordered in monomer A.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 271 - 279 | | Length: | 9 | | Region sequence: |
NALNQLTSR | | Modification type: | Complex
| | PDB: | 1JSC:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (FAD 1 mM; Mg2+ 1 mM; Potassium phosphate 0.2 M; ThDP 1 mM)
| References:
- Pang SS, Duggleby RG, Guddat LW. "Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors." J Mol Biol. 2002; 317(2): 249-62. PubMed: 11902841
| Comments:The mature protein, consisting of residues 58-687, was used for crystal structure determination. A 47 residue N-terminal peptide containing a hexahistidine tag was added.
This region was disordered in monomer A.
|
| Region 3 | | Type: | Disordered | | Name: | | | Location: | 580 - 595 | | Length: | 16 | | Region sequence: |
QGMVTQWQSLFYEHRY | | Modification type: | Complex
| | PDB: | 1JSC:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Modification site
| | Functional subclasses: | Autoregulatory
| Detection methods:
- X-ray crystallography (FAD 1 mM; Mg2+ 1 mM; Potassium phosphate 0.2 M; ThDP 1 mM)
| References:
- Pang SS, Duggleby RG, Guddat LW. "Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors." J Mol Biol. 2002; 317(2): 249-62. PubMed: 11902841
| Comments:The mature protein, consisting of residues 58-687, was used for crystal structure determination. A 47 residue N-terminal peptide containing a hexahistidine tag was added.
This region was traceable in monomer B, but completely disordered in monomer A.
|
| Region 4 | | Type: | Disordered | | Name: | | | Location: | 649 - 687 | | Length: | 39 | | Region sequence: |
VPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH | | Modification type: | Complex
| | PDB: | 1JSC:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Modification site
| | Functional subclasses: | Autoregulatory
| Detection methods:
- X-ray crystallography (FAD 1 mM; Mg2+ 1 mM; Potassium phosphate 0.2 M; ThDP 1 mM)
| References:
- Pang SS, Duggleby RG, Guddat LW. "Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors." J Mol Biol. 2002; 317(2): 249-62. PubMed: 11902841
| Comments:The mature protein, consisting of residues 58-687, was used for crystal structure determination. A 47 residue N-terminal peptide containing a hexahistidine tag was added.
This region is disordered in monomer B, but monomer A contains the additional disordered lysine residue at position 648 in addition to those in monomer B.
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