Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003984 | molecular_function | acetolactate synthase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005948 | cellular_component | acetolactate synthase complex |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009097 | biological_process | isoleucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003984 | molecular_function | acetolactate synthase activity |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005948 | cellular_component | acetolactate synthase complex |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009097 | biological_process | isoleucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue K A 701 |
| Chain | Residue |
| A | GLN343 |
| A | ASP350 |
| A | GLN506 |
| A | TRP508 |
| A | HOH809 |
| A | HOH893 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 702 |
| Chain | Residue |
| A | HOH834 |
| A | HOH891 |
| A | ASP550 |
| A | ASN577 |
| A | TPP703 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue TPP A 703 |
| Chain | Residue |
| A | VAL497 |
| A | GLY498 |
| A | GLN499 |
| A | HIS500 |
| A | GLY523 |
| A | MET525 |
| A | ASP550 |
| A | ALA551 |
| A | SER552 |
| A | ASN577 |
| A | MG702 |
| A | HOH834 |
| A | HOH891 |
| A | HOH948 |
| B | PRO114 |
| B | GLU139 |
| B | PRO165 |
| B | ASN169 |
| B | GLN202 |
| B | ACT712 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue OXY A 704 |
| Chain | Residue |
| A | ALA551 |
| A | GLN600 |
| A | HOH811 |
| A | HOH833 |
| B | TYR113 |
| B | LYS137 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue OXY A 705 |
| Chain | Residue |
| A | GLY115 |
| A | GLY116 |
| A | ALA117 |
| A | THR162 |
| A | SER163 |
| A | GLN202 |
| A | CO2706 |
| A | HOH939 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CO2 A 706 |
| Chain | Residue |
| A | GLY116 |
| A | OXY705 |
| A | HOH939 |
| B | HTL703 |
| B | OXY704 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | binding site for residue FAD A 707 |
| Chain | Residue |
| A | ARG241 |
| A | GLY307 |
| A | ALA308 |
| A | GLY309 |
| A | ASN312 |
| A | THR334 |
| A | LEU335 |
| A | GLN336 |
| A | LEU352 |
| A | GLY353 |
| A | MET354 |
| A | HIS355 |
| A | GLY374 |
| A | ALA375 |
| A | ARG376 |
| A | ASP378 |
| A | ARG380 |
| A | VAL381 |
| A | GLU407 |
| A | VAL408 |
| A | ASN412 |
| A | GLY425 |
| A | ASP426 |
| A | ALA427 |
| A | HOH817 |
| A | HOH829 |
| A | HOH914 |
| A | HOH938 |
| B | PHE201 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue K B 701 |
| Chain | Residue |
| B | GLN343 |
| B | ASP350 |
| B | GLN506 |
| B | TRP508 |
| B | HOH825 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 702 |
| Chain | Residue |
| B | ASP550 |
| B | ASN577 |
| B | HTL703 |
| B | HOH808 |
| B | HOH864 |
| site_id | AD1 |
| Number of Residues | 21 |
| Details | binding site for residue HTL B 703 |
| Chain | Residue |
| B | GLY523 |
| B | MET525 |
| B | GLY549 |
| B | ASP550 |
| B | ALA551 |
| B | SER552 |
| B | ASN577 |
| B | MG702 |
| B | OXY704 |
| B | OXY708 |
| B | HOH808 |
| A | TYR113 |
| A | PRO114 |
| A | GLU139 |
| A | PRO165 |
| A | ASN169 |
| A | GLN202 |
| A | CO2706 |
| B | VAL497 |
| B | GLN499 |
| B | HIS500 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue OXY B 704 |
| Chain | Residue |
| A | CO2706 |
| B | MET582 |
| B | HTL703 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue OXY B 705 |
| Chain | Residue |
| B | GLU578 |
| B | GLN580 |
| B | HIS599 |
| B | GLN600 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue OXY B 706 |
| Chain | Residue |
| A | GLN600 |
| B | TYR113 |
| B | HOH885 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue OXY B 707 |
| Chain | Residue |
| B | GLU578 |
| B | GLN600 |
| B | LEU601 |
| B | ASN602 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue OXY B 708 |
| Chain | Residue |
| B | GLN499 |
| B | MET582 |
| B | HTL703 |
| B | HOH864 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue OXY B 709 |
| Chain | Residue |
| B | GLY115 |
| B | GLY116 |
| B | ALA117 |
| B | THR162 |
| B | SER163 |
| B | GLN202 |
| B | ACT712 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 710 |
| Chain | Residue |
| A | HIS126 |
| B | GLU541 |
| B | HIS597 |
| B | THR598 |
| B | HIS599 |
| site_id | AD9 |
| Number of Residues | 31 |
| Details | binding site for residue FAD B 711 |
| Chain | Residue |
| A | PHE201 |
| B | ARG241 |
| B | GLY307 |
| B | ALA308 |
| B | GLY309 |
| B | ASN312 |
| B | THR334 |
| B | LEU335 |
| B | LEU352 |
| B | MET354 |
| B | HIS355 |
| B | GLY374 |
| B | ALA375 |
| B | ARG376 |
| B | ASP378 |
| B | ARG380 |
| B | VAL381 |
| B | GLU407 |
| B | VAL408 |
| B | ASN412 |
| B | GLY425 |
| B | ASP426 |
| B | ALA427 |
| B | GLN501 |
| B | MET502 |
| B | GLY520 |
| B | GLY521 |
| B | HOH820 |
| B | HOH844 |
| B | HOH852 |
| B | HOH876 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 712 |
| Chain | Residue |
| A | TPP703 |
| B | GLY116 |
| B | GLN202 |
| B | OXY709 |
| B | HOH847 |
Functional Information from PROSITE/UniProt
| site_id | PS00187 |
| Number of Residues | 20 |
| Details | TPP_ENZYMES Thiamine pyrophosphate enzymes signature. IGaqvakPeslvIdIdGDAS |
| Chain | Residue | Details |
| A | ILE533-SER552 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 82 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12496246","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | Region: {"description":"Thiamine pyrophosphate binding"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 289 |
| Chain | Residue | Details |
| A | GLU139 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | PHE201 | single electron acceptor, single electron donor, single electron relay |
| A | GLN202 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS251 | steric locator |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 289 |
| Chain | Residue | Details |
| B | GLU139 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | PHE201 | single electron acceptor, single electron donor, single electron relay |
| B | GLN202 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS251 | steric locator |
| B | MET582 | polar interaction, steric role |
