##gff-version 3 O13437 UniProtKB Chain 1 364 . . . ID=PRO_0000393949;Note=Formate dehydrogenase O13437 UniProtKB Binding site 93 93 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Binding site 119 119 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Binding site 174 175 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Binding site 195 195 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Binding site 230 234 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Binding site 256 256 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Binding site 282 282 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Binding site 311 314 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|HAMAP-Rule:MF_03210 O13437 UniProtKB Site 258 258 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03210,ECO:0000305|PubMed:17525463;Dbxref=PMID:17525463 O13437 UniProtKB Site 311 311 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_03210,ECO:0000305|PubMed:17525463;Dbxref=PMID:17525463 O13437 UniProtKB Natural variant 9 9 . . . Note=In strain: 2.2159. D->G;Ontology_term=ECO:0000305,ECO:0000312;evidence=ECO:0000305,ECO:0000312|EMBL:ABE69165.2 O13437 UniProtKB Natural variant 50 51 . . . Note=In strain: 2.2159 and NCYC 1513. ET->GN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Natural variant 53 53 . . . Note=In strain: 2.2159 and NCYC 1513. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Natural variant 56 56 . . . Note=In strain: 2.2159 and NCYC 1513. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Natural variant 79 79 . . . Note=In strain: 2.2159 and NCYC 1513. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Natural variant 84 84 . . . Note=In strain: 2.2159 and NCYC 1513. N->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Natural variant 87 87 . . . Note=In strain: ATCC 56294 / CBS 8030 / CCRC 21757 / NRRLY-17325. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7557425;Dbxref=PMID:7557425 O13437 UniProtKB Natural variant 108 108 . . . Note=In strain: 2.2159. K->R;Ontology_term=ECO:0000305,ECO:0000312;evidence=ECO:0000305,ECO:0000312|EMBL:ABE69165.2 O13437 UniProtKB Natural variant 145 145 . . . Note=In strain: 2.2159. I->N;Ontology_term=ECO:0000305,ECO:0000312;evidence=ECO:0000305,ECO:0000312|EMBL:ABE69165.2 O13437 UniProtKB Natural variant 184 184 . . . Note=In strain: 2.2159 and NCYC 1513. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Natural variant 202 202 . . . Note=In strain: 2.2159 and NCYC 1513. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Natural variant 308 308 . . . Note=In strain: 2.2159. M->T;Ontology_term=ECO:0000305,ECO:0000312;evidence=ECO:0000305,ECO:0000312|EMBL:ABE69165.2 O13437 UniProtKB Natural variant 325 325 . . . Note=In strain: 2.2159 and NCYC 1513. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 23 23 . . . Note=Slight increase in substrate affinity for formate but no change in affinity for NAD%2C 9 degrees Celsius decrease in thermal stability compared to the wild-type%2C significantly higher stability compared to wild-type under biotransformation conditions%2C significantly more stable in the presence of CuCl(2)%3B when associated with A-262. Large increase in substrate affinity for formate but no significant change in affinity for NAD%2C 13 degrees Celsius decrease in thermal stability compared to the wild-type%2C significantly more stable in the presence of CuCl(2)%3B when associated with V-262. No significant change in affinity for formate or NAD%2C 5 degrees Celsius decrease in thermal stability compared to the wild-type%2C significantly higher stability compared to wild-type under biotransformation conditions%2C and significantly more stable in the presence of CuCl(2). C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10691964;Dbxref=PMID:10691964 O13437 UniProtKB Mutagenesis 47 47 . . . Note=Slight increase in substrate affinity for formate and also affinity for NAD increases by half after 2 weeks. Also after 4 months affinity for formate increases by more than half and affinity for NAD increases by more than half. Retains 84%25 of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50%25 of its activity at 55 degrees Celsius. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17525463;Dbxref=PMID:17525463 O13437 UniProtKB Mutagenesis 69 69 . . . Note=2-fold decrease in substrate affinity for formate%2C but no significant change in affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 119 119 . . . Note=94-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type%3B when associated with A-311. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 119 119 . . . Note=80-fold decrease in substrate affinity for formate and a 1250-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. N->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 175 175 . . . Note=2-fold decrease in substrate affinity for formate and a 12-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 197 197 . . . Note=4-fold decrease in substrate affinity for formate but no significant change in affinity for NAD compared to the wild-type. Q->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 258 258 . . . Note=No catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 262 262 . . . Note=Slight increase in substrate affinity for formate but no change in affinity for NAD%2C 9 degrees Celsius decrease in thermal stability compared to the wild-type%2C greater stability at a higher pH compared to the wild-type%3B when associated with S-23. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10691964;Dbxref=PMID:10691964 O13437 UniProtKB Mutagenesis 262 262 . . . Note=Large increase in substrate affinity for formate but no significant change in affinity for NAD%2C 13 degrees Celsius decrease in thermal stability compared to the wild-type%3B when associated with S-23. Great increase in substrate affinity for formate and NAD and 8 degrees Celsius decrease in thermal stability compared to the wild-type. C->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10691964;Dbxref=PMID:10691964 O13437 UniProtKB Mutagenesis 287 287 . . . Note=2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type%3B when associated with A-311. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 287 287 . . . Note=380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type%3B when associated with T-288. No significant decrease in substrate affinity for formate but a 4-fold decrease in substrate affinity for NAD and a significant reduction in catalytic activity compared to the wild-type%2C a more acidic pH is seen than in the wild-type%2C preventing formate binding by a single ionization of a group compared to that of the wild-type. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 288 288 . . . Note=380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type%3B when associated with E-287. P->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 311 311 . . . Note=2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type%3B when associated with A-287. 93-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD%2C and a significant reduction in catalytic activity compared to the wild-type%3B when associated with A-119. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 311 311 . . . Note=10-fold decrease in substrate affinity for formate and significant reduction in the catalytic activity compared to the wild-type. H->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11171126;Dbxref=PMID:11171126 O13437 UniProtKB Mutagenesis 328 328 . . . Note=A 75%25 increase in substrate affinity for formate after 2 weeks and a 50%25 increase in affinity for NAD. However%2C after 4 months the affinity for formate increases 7-fold and affinity for NAD increases by 2 thirds. Retains 70%25 of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50%25 of its activity at 55 degrees Celsius. K->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17525463;Dbxref=PMID:17525463 O13437 UniProtKB Mutagenesis 360 360 . . . Note=Exhibits no change in substrate affinity for formate%2C but shows a 4-fold decrease in substrate affinity for NAD implying that L-360 side chain forms strong interactions with the cofactor. A higher reaction rate is observed at an acidic and basic pH values. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11054119;Dbxref=PMID:11054119 O13437 UniProtKB Sequence conflict 19 23 . . . Note=KLYGC->EKLYG;Ontology_term=ECO:0000305;evidence=ECO:0000305 O13437 UniProtKB Sequence conflict 23 23 . . . Note=C->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 O13437 UniProtKB Beta strand 2 6 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 12 16 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Turn 24 26 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 31 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 49 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2FSS O13437 UniProtKB Helix 53 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 58 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 62 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 76 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 87 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 100 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 111 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 120 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 138 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 152 156 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 166 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 174 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 184 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 189 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 201 206 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 209 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 215 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 223 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Turn 233 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 241 244 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 251 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 259 261 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 264 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 275 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 285 288 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 294 297 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 306 308 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 313 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 317 335 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Helix 343 345 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I O13437 UniProtKB Beta strand 346 349 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J6I