ACL_RS02300
  | Uniprot: A9NFE9
Description: acetyl-CoA carboxylase carboxyltransferase subunit alpha EC number: 6.4.1.2 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS00057344}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS00177034}. Pathway: PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS00057363}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): accA Gene names (synonym): Mass: 30,618 Subunit structure [CC]: SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD). {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS00176983}. Gene ontology (GO): acetyl-CoA carboxylase complex [GO:0009317]; acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; fatty acid biosynthetic process [GO:0006633]; malonyl-CoA biosynthetic process [GO:2001295] Gene ontology IDs: GO:0003989; GO:0005524; GO:0006633; GO:0009317; GO:2001295 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the AccA family. {ECO:0000256|HAMAP-Rule:MF_00823, ECO:0000256|SAAS:SAAS00558839}. Protein families: AccA family Coiled coil: Domain [FT]: DOMAIN 1 252 COA_CT_CTER. {ECO:0000259|PROSITE:PS50989}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NFE9 MEROPS: EnsemblBacteria KO: ABX81079 UniPathway: K01962 CDD: Gene3D: HAMAP: 3.90.226.10 InterPro: MF_00823 PANTHER: IPR001095;IPR029045;IPR011763 PIRSF: PRINTS: PROSITE: PR01069 Pfam: PS50989 ProDom: PF03255 SMART: SUPFAM: TIGRFAMs: SSF52096 |
485774-486608(+) >nucleotide sequence ACATCAAAGTCACTTATTAAAGCAATCTTCCCTGATTTCATTGAACTACATGGTGATCGT CTTTACGGCGATGATGAAGCTATTGTAGGTGGACTGGCGACCTTTAATGATATACCAGTT ACGGTGATTGCTGAAGAAAAGGGTACTGATACACAAAATAGATTAAAACATAATTTTGGT ATGCCACATCCTGAAGGTTATCGTAAGGCATTAAGATTGATGAAACAAGCCGAGAAGTTT AAACGTCCTATTATTACAATTATTGATACACCAGGTGCTTATCCGGGACTTGGCGCAGAA GAACGTGGCCAAGCAGGTGCGATTGCATTAAATTTAAAAGAACTGATGGTGTTAAAAACA CCTATTATTGTTATTGTATTAGGTGAAGGTGGTTCTGGTGGTGCACTTGCTATAGGTGTA GGCGATCACATTATGATGTTTGAAAATGCGATATATTCTATATTATCACCTGAAGGATTT GCTTCAATTTTATTTAAAGATAGTACACGTGCTAATGAGGCTGCTCATTTAATGAAACTT ACAGCAGAAGATTTAAAATCATTTGGTATTATTGATGAAATCATCTTAGAGGGTAAGGGA TTAAATACAGACCCTGAAGTCGGTTATACCAATTTAAAGAAACAAATAAGTAAACAACTA ACAAAATTAATGAAAACACCTGTAGAAAAACTTCTTGTTAATAGATATGACAAGTTCAAA AAAATGGGTGAATACGAAGAAAGTGTGATCAAAAATGAAGAACTTGCCGATTAA >protein sequence TVIAEEKGTDTQNRLKHNFGMPHPEGYRKALRLMKQAEKFKRPIITIIDTPGAYPGLGAE ERGQAGAIALNLKELMVLKTPIIVIVLGEGGSGGALAIGVGDHIMMFENAIYSILSPEGF ASILFKDSTRANEAAHLMKLTAEDLKSFGIIDEIILEGKGLNTDPEVGYTNLKKQISKQL TKLMKTPVEKLLVNRYDKFKKMGEYEESVIKNEELAD |
© Fisunov Lab of Proteomics, 2016.