1T90
Crystal structure of methylmalonate semialdehyde dehydrogenase from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
A | 0006210 | biological_process | thymine catabolic process |
A | 0006574 | biological_process | valine catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0018478 | molecular_function | malonate-semialdehyde dehydrogenase (acetylating) activity |
A | 0019310 | biological_process | inositol catabolic process |
B | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
B | 0006210 | biological_process | thymine catabolic process |
B | 0006574 | biological_process | valine catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0018478 | molecular_function | malonate-semialdehyde dehydrogenase (acetylating) activity |
B | 0019310 | biological_process | inositol catabolic process |
C | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
C | 0006210 | biological_process | thymine catabolic process |
C | 0006574 | biological_process | valine catabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0018478 | molecular_function | malonate-semialdehyde dehydrogenase (acetylating) activity |
C | 0019310 | biological_process | inositol catabolic process |
D | 0004491 | molecular_function | methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity |
D | 0006210 | biological_process | thymine catabolic process |
D | 0006574 | biological_process | valine catabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0018478 | molecular_function | malonate-semialdehyde dehydrogenase (acetylating) activity |
D | 0019310 | biological_process | inositol catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 1490 |
Chain | Residue |
A | ILE149 |
A | HIS209 |
A | VAL212 |
A | PHE226 |
A | VAL227 |
A | GLY228 |
A | SER229 |
A | VAL232 |
A | LEU250 |
A | THR251 |
A | GLY252 |
A | ALA150 |
A | CYS284 |
A | GLU382 |
A | PHE384 |
A | ASN410 |
A | PHE449 |
A | HOH1504 |
A | HOH1617 |
A | HOH1661 |
A | HOH1692 |
A | PRO151 |
A | PHE152 |
A | ASN153 |
A | TRP161 |
A | LYS176 |
A | GLU179 |
A | ARG180 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 2490 |
Chain | Residue |
B | ILE149 |
B | ALA150 |
B | PRO151 |
B | PHE152 |
B | ASN153 |
B | TRP161 |
B | LYS176 |
B | GLU179 |
B | ARG180 |
B | HIS209 |
B | VAL212 |
B | PHE226 |
B | VAL227 |
B | GLY228 |
B | SER229 |
B | VAL232 |
B | LEU250 |
B | THR251 |
B | GLY252 |
B | CYS284 |
B | GLU382 |
B | PHE384 |
B | ASN410 |
B | PHE449 |
B | HOH2514 |
B | HOH2703 |
B | HOH2719 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD C 3490 |
Chain | Residue |
C | ILE149 |
C | ALA150 |
C | PRO151 |
C | PHE152 |
C | ASN153 |
C | TRP161 |
C | LYS176 |
C | GLU179 |
C | HIS209 |
C | VAL212 |
C | PHE226 |
C | VAL227 |
C | GLY228 |
C | SER229 |
C | VAL232 |
C | LEU250 |
C | THR251 |
C | GLY252 |
C | CYS284 |
C | GLU382 |
C | PHE384 |
C | ASN410 |
C | PHE449 |
C | HOH3498 |
C | HOH3572 |
C | HOH3701 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD D 4490 |
Chain | Residue |
D | GLY252 |
D | CYS284 |
D | GLU382 |
D | PHE384 |
D | ASN410 |
D | PHE449 |
D | HOH4497 |
D | HOH4514 |
D | HOH4594 |
D | ILE149 |
D | ALA150 |
D | PRO151 |
D | PHE152 |
D | ASN153 |
D | TRP161 |
D | LYS176 |
D | GLU179 |
D | ARG180 |
D | HIS209 |
D | VAL212 |
D | PHE226 |
D | VAL227 |
D | GLY228 |
D | SER229 |
D | VAL232 |
D | LEU250 |
D | THR251 |
Functional Information from PROSITE/UniProt
site_id | PS00070 |
Number of Residues | 12 |
Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FgSAGERCMACA |
Chain | Residue | Details |
A | PHE277-ALA288 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P25526, ECO:0000255|HAMAP-Rule:MF_01670 |
Chain | Residue | Details |
A | CYS284 | |
B | CYS284 | |
C | CYS284 | |
D | CYS284 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15272169, ECO:0007744|PDB:1T90 |
Chain | Residue | Details |
A | ALA150 | |
B | PHE152 | |
B | LYS176 | |
B | GLU179 | |
B | ARG180 | |
B | SER229 | |
B | THR251 | |
B | GLU382 | |
C | ALA150 | |
C | PHE152 | |
C | LYS176 | |
A | PHE152 | |
C | GLU179 | |
C | ARG180 | |
C | SER229 | |
C | THR251 | |
C | GLU382 | |
D | ALA150 | |
D | PHE152 | |
D | LYS176 | |
D | GLU179 | |
D | ARG180 | |
A | LYS176 | |
D | SER229 | |
D | THR251 | |
D | GLU382 | |
A | GLU179 | |
A | ARG180 | |
A | SER229 | |
A | THR251 | |
A | GLU382 | |
B | ALA150 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
A | CYS284 | |
A | ASN153 | |
A | LEU250 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
B | CYS284 | |
B | ASN153 | |
B | LEU250 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
C | CYS284 | |
C | ASN153 | |
C | LEU250 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a4s |
Chain | Residue | Details |
D | CYS284 | |
D | ASN153 | |
D | LEU250 |