##gff-version 3 Q8K009 UniProtKB Chain 1 923 . . . ID=PRO_0000316002;Note=Mitochondrial 10-formyltetrahydrofolate dehydrogenase Q8K009 UniProtKB Transit peptide 1 19 . . . Note=Mitochondrion%3B not cleaved;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3SY69 Q8K009 UniProtKB Domain 339 416 . . . Note=Carrier;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00258 Q8K009 UniProtKB Region 23 331 . . . Note=Hydrolase domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Region 438 923 . . . Note=Aldehyde dehydrogenase domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Active site 128 128 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Active site 694 694 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Active site 728 728 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Binding site 110 112 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75891 Q8K009 UniProtKB Binding site 164 164 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75891 Q8K009 UniProtKB Binding site 592 594 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Binding site 618 621 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Binding site 651 656 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Binding site 671 672 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Binding site 694 695 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Binding site 778 778 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Binding site 825 827 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Site 164 164 . . . Note=Essential for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P28037 Q8K009 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75891 Q8K009 UniProtKB Modified residue 60 60 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8R0Y6 Q8K009 UniProtKB Modified residue 375 375 . . . Note=O-(pantetheine 4'-phosphoryl)serine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q3SY69,ECO:0000255|PROSITE-ProRule:PRU00258 Q8K009 UniProtKB Modified residue 650 650 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75891 Q8K009 UniProtKB Modified residue 681 681 . . . Note=N6-succinyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q8K009 UniProtKB Modified residue 903 903 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3SY69 Q8K009 UniProtKB Sequence conflict 476 476 . . . Note=Y->H;Ontology_term=ECO:0000305;evidence=ECO:0000305