##gff-version 3 Q28559 UniProtKB Chain 1 2346 . . . ID=PRO_0000146766;Note=Acetyl-CoA carboxylase 1 Q28559 UniProtKB Domain 117 618 . . . Note=Biotin carboxylation;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Domain 275 466 . . . Note=ATP-grasp;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q28559 UniProtKB Domain 745 819 . . . Note=Biotinyl-binding;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01066 Q28559 UniProtKB Domain 1576 1914 . . . Note=CoA carboxyltransferase N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01136 Q28559 UniProtKB Domain 1918 2234 . . . Note=CoA carboxyltransferase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01137 Q28559 UniProtKB Region 1576 2234 . . . Note=Carboxyltransferase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01138 Q28559 UniProtKB Active site 441 441 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q28559 UniProtKB Binding site 315 320 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409 Q28559 UniProtKB Binding site 424 424 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 424 424 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 437 437 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 437 437 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 437 437 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 437 437 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 439 439 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 439 439 . . . Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00409,ECO:0000255|PROSITE-ProRule:PRU00969 Q28559 UniProtKB Binding site 1823 1823 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q28559 UniProtKB Binding site 2127 2127 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q28559 UniProtKB Binding site 2129 2129 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q28559 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 5 5 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 23 23 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 25 25 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11497 Q28559 UniProtKB Modified residue 48 48 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 50 50 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11497 Q28559 UniProtKB Modified residue 53 53 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 58 58 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SWU9 Q28559 UniProtKB Modified residue 78 78 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11497 Q28559 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine%3B by AMPK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SWU9 Q28559 UniProtKB Modified residue 610 610 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 786 786 . . . Note=N6-biotinyllysine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P11497,ECO:0000255|PROSITE-ProRule:PRU01066 Q28559 UniProtKB Modified residue 835 835 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 1201 1201 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11497 Q28559 UniProtKB Modified residue 1216 1216 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11497 Q28559 UniProtKB Modified residue 1218 1218 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SWU9 Q28559 UniProtKB Modified residue 1227 1227 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SWU9 Q28559 UniProtKB Modified residue 1259 1259 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SWU9 Q28559 UniProtKB Modified residue 1263 1263 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 1273 1273 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 1334 1334 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Modified residue 2153 2153 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13085 Q28559 UniProtKB Alternative sequence 1 75 . . . ID=VSP_026102;Note=In isoform 2. MGEPSSLAKPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVSSDTLSDLGISSLQDGLALHM->MEGSAEESKEMRYYMLQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9639557;Dbxref=PMID:9639557 Q28559 UniProtKB Alternative sequence 1 1 . . . ID=VSP_026103;Note=In isoform 3. M->MWWSTLMSILRASSFWKWISAQTIRIIRALRARFEGTM;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15607423;Dbxref=PMID:15607423