1REQ
METHYLMALONYL-COA MUTASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
A | 0005515 | molecular_function | protein binding |
A | 0016853 | molecular_function | isomerase activity |
A | 0016866 | molecular_function | intramolecular transferase activity |
A | 0031419 | molecular_function | cobalamin binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0016853 | molecular_function | isomerase activity |
B | 0016866 | molecular_function | intramolecular transferase activity |
B | 0019652 | biological_process | lactate fermentation to propionate and acetate |
B | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
B | 0031419 | molecular_function | cobalamin binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
C | 0005515 | molecular_function | protein binding |
C | 0016853 | molecular_function | isomerase activity |
C | 0016866 | molecular_function | intramolecular transferase activity |
C | 0031419 | molecular_function | cobalamin binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004494 | molecular_function | methylmalonyl-CoA mutase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0016853 | molecular_function | isomerase activity |
D | 0016866 | molecular_function | intramolecular transferase activity |
D | 0019652 | biological_process | lactate fermentation to propionate and acetate |
D | 0019678 | biological_process | propionate metabolic process, methylmalonyl pathway |
D | 0031419 | molecular_function | cobalamin binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 46 |
Details | BINDING SITE FOR RESIDUE B12 A 800 |
Chain | Residue |
A | TYR89 |
A | GLY333 |
A | TRP334 |
A | LEU336 |
A | GLU370 |
A | ALA371 |
A | ALA373 |
A | LEU374 |
A | GLN454 |
A | LEU602 |
A | GLY609 |
A | ALA116 |
A | HIS610 |
A | ASP611 |
A | ARG612 |
A | GLY613 |
A | ILE617 |
A | TYR621 |
A | SER655 |
A | LEU657 |
A | ALA658 |
A | GLY659 |
A | PHE117 |
A | GLY685 |
A | GLY686 |
A | TYR705 |
A | THR706 |
A | THR709 |
A | GOL802 |
A | HOH825 |
A | HOH886 |
A | HOH893 |
A | HOH896 |
A | LEU119 |
A | HOH923 |
A | HOH962 |
A | HOH985 |
A | HOH988 |
A | HOH994 |
A | HOH1052 |
A | HOH1075 |
A | ALA139 |
A | VAL206 |
A | ARG207 |
A | TYR243 |
A | GLU247 |
site_id | AC2 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE DCA A 801 |
Chain | Residue |
A | TYR75 |
A | THR77 |
A | MET78 |
A | ARG82 |
A | THR85 |
A | ARG87 |
A | SER114 |
A | SER164 |
A | THR166 |
A | THR195 |
A | ASN236 |
A | ARG283 |
A | SER285 |
A | PHE287 |
A | ARG326 |
A | THR327 |
A | HIS328 |
A | GLN361 |
A | SER362 |
A | HOH808 |
A | HOH809 |
A | HOH828 |
A | HOH837 |
A | HOH838 |
A | HOH839 |
A | HOH843 |
A | HOH869 |
A | HOH889 |
A | HOH895 |
A | HOH906 |
A | HOH977 |
A | HOH984 |
A | HOH1011 |
B | VAL42 |
B | ARG45 |
site_id | AC3 |
Number of Residues | 46 |
Details | BINDING SITE FOR RESIDUE B12 C 800 |
Chain | Residue |
C | GLY609 |
C | HIS610 |
C | ASP611 |
C | ARG612 |
C | GLY613 |
C | ILE617 |
C | TYR621 |
C | GLY653 |
C | SER655 |
C | LEU657 |
C | GLY659 |
C | GLY685 |
C | GLY686 |
C | TYR705 |
C | THR706 |
C | THR709 |
C | GOL802 |
C | HOH887 |
C | HOH894 |
C | HOH897 |
C | HOH924 |
C | HOH961 |
C | HOH984 |
C | HOH994 |
C | HOH1055 |
C | HOH1059 |
C | HOH1081 |
C | HOH1141 |
C | TYR89 |
C | PHE117 |
C | LEU119 |
C | HIS122 |
C | ALA139 |
C | VAL206 |
C | ARG207 |
C | THR209 |
C | GLU247 |
C | GLY333 |
C | TRP334 |
C | LEU336 |
C | GLU370 |
C | ALA371 |
C | ALA373 |
C | LEU374 |
C | GLN454 |
C | LEU602 |
site_id | AC4 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE DCA C 801 |
Chain | Residue |
C | TYR75 |
C | THR77 |
C | MET78 |
C | ARG82 |
C | THR85 |
C | ARG87 |
C | SER114 |
C | SER164 |
C | THR166 |
C | THR195 |
C | ASN236 |
C | ARG283 |
C | SER285 |
C | ARG326 |
C | THR327 |
C | HIS328 |
C | GLN361 |
C | SER362 |
C | HOH808 |
C | HOH809 |
C | HOH829 |
C | HOH838 |
C | HOH839 |
C | HOH840 |
C | HOH844 |
C | HOH871 |
C | HOH890 |
C | HOH896 |
C | HOH907 |
C | HOH976 |
C | HOH983 |
C | HOH1013 |
C | HOH1221 |
C | HOH1271 |
D | ARG45 |
D | HOH1380 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 802 |
Chain | Residue |
A | TYR89 |
A | ARG207 |
A | TYR243 |
A | GLN330 |
A | B12800 |
A | HOH845 |
A | HOH1138 |
A | HOH1254 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 1 |
Chain | Residue |
B | GLU114 |
B | ARG169 |
B | ASN239 |
B | ASN243 |
B | TRP328 |
B | GLN365 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 639 |
Chain | Residue |
B | THR98 |
B | ARG100 |
B | ALA106 |
B | TRP107 |
B | GLY354 |
B | ALA355 |
B | HOH810 |
B | HOH859 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 803 |
Chain | Residue |
A | GLU42 |
A | ALA250 |
A | THR251 |
A | HOH804 |
A | HOH805 |
A | HOH920 |
A | HOH927 |
A | HOH980 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 640 |
Chain | Residue |
B | ARG329 |
B | ASN446 |
B | ARG449 |
B | HIS491 |
B | ASP493 |
B | HOH873 |
B | HOH886 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 802 |
Chain | Residue |
C | TYR89 |
C | ARG207 |
C | TYR243 |
C | GLN330 |
C | B12800 |
C | HOH846 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 1 |
Chain | Residue |
D | GLU114 |
D | ARG169 |
D | ASN239 |
D | ASN243 |
D | TRP328 |
D | GLN365 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 803 |
Chain | Residue |
C | ALA41 |
C | GLU42 |
C | THR251 |
C | HOH804 |
C | HOH805 |
C | HOH921 |
C | HOH928 |
C | HOH1148 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 639 |
Chain | Residue |
D | ASN446 |
D | ARG449 |
D | ALA450 |
D | LEU453 |
D | HIS491 |
D | ARG492 |
D | ASP493 |
D | HOH1459 |
Functional Information from PROSITE/UniProt
site_id | PS00544 |
Number of Residues | 26 |
Details | METMALONYL_COA_MUTASE Methylmalonyl-CoA mutase signature. RIARNTgiVLaEEvnigRvnDPaGGS |
Chain | Residue | Details |
B | ARG377-SER402 | |
A | ARG381-SER406 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10387043, ECO:0007744|PDB:4REQ |
Chain | Residue | Details |
A | ALA76 | |
A | MET245 | |
A | LEU284 | |
A | PHE286 | |
C | ALA76 | |
C | TYR79 | |
C | PRO83 | |
C | ILE86 | |
C | GLN88 | |
C | ALA90 | |
C | VAL115 | |
A | TYR79 | |
C | ILE196 | |
C | ASN198 | |
C | MET245 | |
C | LEU284 | |
C | PHE286 | |
A | PRO83 | |
A | ILE86 | |
A | GLN88 | |
A | ALA90 | |
A | VAL115 | |
A | ILE196 | |
A | ASN198 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10387043, ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ, ECO:0007744|PDB:4REQ |
Chain | Residue | Details |
A | ASP118 | |
A | GLY613 | |
A | SER656 | |
A | ALA658 | |
A | VAL687 | |
A | VAL710 | |
C | ASP118 | |
C | GLY140 | |
C | ARG207 | |
C | ASN208 | |
C | TRP334 | |
A | GLY140 | |
C | ALA371 | |
C | LEU374 | |
C | HIS610 | |
C | ARG612 | |
C | GLY613 | |
C | SER656 | |
C | ALA658 | |
C | VAL687 | |
C | VAL710 | |
A | ARG207 | |
A | ASN208 | |
A | TRP334 | |
A | ALA371 | |
A | LEU374 | |
A | HIS610 | |
A | ARG612 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:10387043, ECO:0000269|PubMed:8805541, ECO:0007744|PDB:1REQ, ECO:0007744|PDB:4REQ |
Chain | Residue | Details |
A | ASP611 | |
C | ASP611 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:9772164 |
Chain | Residue | Details |
A | ALA90 | |
C | ALA90 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 11456766, 8805541, 10387043 |
Chain | Residue | Details |
A | ASP608 | |
A | LYS604 | |
A | TYR89 | |
A | HIS244 | |
A | HIS610 |
site_id | CSA2 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 11456766, 8805541, 10387043 |
Chain | Residue | Details |
C | ASP608 | |
C | LYS604 | |
C | TYR89 | |
C | HIS244 | |
C | HIS610 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 62 |
Chain | Residue | Details |
A | ALA90 | electrostatic stabiliser, radical stabiliser |
A | HIS244 | electrostatic stabiliser, radical stabiliser |
A | MET245 | electrostatic stabiliser, proton acceptor, proton donor |
A | MET605 | electrostatic stabiliser |
A | GLY609 | electrostatic stabiliser |
A | ASP611 | metal ligand |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 62 |
Chain | Residue | Details |
C | ALA90 | electrostatic stabiliser, radical stabiliser |
C | HIS244 | electrostatic stabiliser, radical stabiliser |
C | MET245 | electrostatic stabiliser, proton acceptor, proton donor |
C | MET605 | electrostatic stabiliser |
C | GLY609 | electrostatic stabiliser |
C | ASP611 | metal ligand |