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0COA1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameACACA
DescriptionAcetyl-coa carboxylase 1 (ec 6.4.1.2) (acc-alpha) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0003989 acetyl-CoA carboxylase activity (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This region is found in various eukaryotic acetyl-CoA carboxylases.-terminal to the catalytic domain (). This enzyme () is involved in the synthesis of long-chain fatty acids.s it catalyses the rate limiting step in this process.
  IPR013537:Acetyl-CoA carboxylase, central region
Members in this domain include biotin dependent carboxylases.The carboxyl transferase domain carries out the following reaction;transcarboxylation from biotin to an acceptor molecule. There aretwo recognised types of carboxyl transferase. One of them uses acyl-CoAand the other uses 2-oxo acid as the acceptor molecule of carbon dioxide. All of the members in this family utilise acyl-CoA as the acceptormolecule.
  IPR000022:Carboxyl transferase
Carbamoyl-phosphate synthase (CPSase) catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine () or ammonia () and bicarbonate . This important enzyme initiates both the urea cycle and the biosynthesis of arginine and pyrimidines. Glutamine-dependent CPSase (CPSase II) is involved in the biosynthesis of pyrimidines and purines. In bacteria such as Escherichia coli. single enzyme is involved in both biosynthetic pathways while other bacteria have separate enzymes. The bacterial enzymes are formed of two subunits. A small chain (carA) that provides glutamine amidotransferase activity (GATase) necessary for removal of the ammonia group from glutamine.nd a large chain (carB)that provides CPSase activity. Such a structure is also present in fungi for arginine biosynthesis (CPA1 and CPA2). Two main CPSases have been identified in mammals.PSase I is mitochondrial.s found in high levels in the liver and is involved in arginine biosynthesis; while CPSase II is cytosolic.s associated with aspartate carbamoyltransferase (ATCase) and dihydroorotase (DHOase) and is involved in pyrimidine biosynthesis. In the pyrimidine pathway in most eukaryotes.PSase is found as a domain in a multi-functional protein.hich also has GATase.CTase and DHOase activity. Ammonia-dependent CPSase (CPSase I) is involved in the urea cycle in ureolytic vertebrates and is a monofunctional protein located in the mitochondrial matrix. The CPSase domain is typically 120 kD in size and has arisen from the duplication of an ancestral subdomain of about 500 amino acids. Each subdomain independently binds to ATP and it is suggested that the two homologous halves act separately.ne to catalyze the phosphorylation of bicarbonate to carboxyphosphate and the other that of carbamate to carbamyl phosphate. The CPSase subdomain is also present in a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase () (ACC).ropionyl-CoA carboxylase () (PCCase).yruvate carboxylase () (PC) and urea carboxylase().
  IPR005479:Carbamoyl-phosphate synthase L chain, ATP-binding
Carbamoyl-phosphate synthase (CPSase) catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine () or ammonia () and bicarbonate . This important enzyme initiates both the urea cycle and the biosynthesis of arginine and pyrimidines. Glutamine-dependent CPSase (CPSase II) is involved in the biosynthesis of pyrimidines and purines. In bacteria such as Escherichia coli. single enzyme is involved in both biosynthetic pathways while other bacteria have separate enzymes. The bacterial enzymes are formed of two subunits. A small chain (carA) that provides glutamine amidotransferase activity (GATase) necessary for removal of the ammonia group from glutamine.nd a large chain (carB)that provides CPSase activity. The large subunit consists of four structural units: the carboxyphosphate synthetic component.he oligomerization domain.he carbamoyl phosphate synthetic component and the allosteric domain . Such a structure is also present in fungi for arginine biosynthesis (CPA1 and CPA2). Such a structure is also present in fungi for arginine biosynthesis (CPA1 and CPA2). Two main CPSases have been identified in mammals.PSase I is mitochondrial.s found in high levels in the liver and is involved in arginine biosynthesis; while CPSase II is cytosolic.s associated with aspartate carbamoyltransferase (ATCase) and dihydroorotase (DHOase) and is involved in pyrimidine biosynthesis. In the pyrimidine pathway in most eukaryotes.PSase is found as a domain in a multi-functional protein.hich also has GATase.CTase and DHOase activity. Ammonia-dependent CPSase (CPSase I) is involved in the urea cycle in ureolytic vertebrates and is a monofunctional protein located in the mitochondrial matrix. The CPSase domain is typically 120 kD in size and has arisen from the duplication of an ancestral subdomain of about 500 amino acids. Each subdomain independently binds to ATP and it is suggested that the two homologous halves act separately.ne to catalyze the phosphorylation of bicarbonate to carboxyphosphate and the other that of carbamate to carbamyl phosphate. The CPSase subdomain is also present in a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase () (ACC).ropionyl-CoA carboxylase () (PCCase).yruvate carboxylase () (PC) and urea carboxylase().
  IPR005481:Carbamoyl-phosphate synthetase large chain, N-terminal
Acetyl-CoA carboxylase is found in all animals.lants.nd bacteria and catalyzes the first committed step in fatty acid synthesis. It is a multicomponent enzyme containing a biotin carboxylase activity. biotin carboxyl carrier protein.nd a carboxyltransferase functionality. The "B-domain" extends from the main body of the subunit where it folds into two alpha-helical regions and three strands of beta-sheet. Following the excursion into the B-domain.he polypeptide chain folds back into the body of the protein where it forms an eight-stranded antiparallel beta-sheet. In addition to this major secondary structural element.he C-terminal domain also contains a smaller three-stranded antiparallel beta-sheet and seven alpha-helices .
  IPR005482:Biotin carboxylase, C-terminal
The biotin / lipoyl attachment domain has a conserved lysine residue that binds biotin or lipoicacid. Biotin plays a catalytic role in some carboxyl transfer reactions and is covalently attached.ia an amide bond.o a lysine residue in enzymes requiring this coenzyme . E2 acyltransferases have an essential cofactor.ipoic acid.hich is covalently bound via an amide linkage to a lysine group . The lipoic acid cofactor is found in a variety of proteins that include.-protein of the glycine cleavage system (GCS).ammalian and yeast pyruvate dehydrogenases and fast migrating protein (FMP) (gene acoC) from Alcaligenes eutrophus.
  IPR000089:Biotin/lipoyl attachment
The ATP-grasp fold is one of several distinct ATP-binding folds.nd is found in enzymes that catalyze the formation of amide bonds.atalyzing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule . This fold is found in many different enzyme families.ncluding various peptide synthetases.iotin carboxylase.ynapsin.uccinyl-CoA synthetase.yruvate phosphate dikinase.nd glutathione synthetase.mongst others . These enzymes contribute predominantly to macromolecular synthesis.sing ATP-hydrolysis to activate their substrates. This entry represents the pre-ATP-grasp domain.hich precedes the ATP-grasp domain in all superfamily members.nd which usually occurs at the N-terminus of the protein. The structure of the pre-ATP-grasp domain consists of alpha/beta/alpha in three layers.nd is possibly a rudiment form of the Rossmann-fold. This domain can have a substrate-binding function.
  IPR013817:Pre-ATP-grasp fold
The single hybrid motif has a beta-barrel sandwich hybrid fold.onsisting of a sandwich of half-barrel shaped beta-sheets. This motif is found in biotinyl/lipoyl-carrier proteins and domains.here the biotin and lipoic acid moieties act as covalently attached coenzyme cofactors in enzymes that catalyse metabolic reactions. For example.his motif can be found in the biotinyl domain of Escherichia coli acetyl-CoA carboxylase .rotein H of the glycine cleavage system in Pisum sativum .he ipoyl domain of dihydrolipoamide acetyltransferase.hich is a component of the pyruvate dehydrogenase complex .he lipoyl domain of the 2-oxoglutarate dehydrogenase complex .nd the lipoyl domain f the mitochondrial branched-chain alpha-ketoacid dehydrogenase.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011053:Single hybrid motif
The rudiment single hybrid motif has a beta-barrel sandwich hybrid motif.onsisting of a sandwich of half-barrel shaped beta-sheets. This motif is found in the small domain of cytochrome f .s well as in the C-terminal domain of the biotin carboxylase subunit of acetyl-CoA carboxylase .nd its family members.uch as glycinamide ribonucleotide synthetase C-terminal domain .5-carboxyaminoimidazole ribonucleotide synthetase PurK C-terminal domain .nd glycinamide ribonucleotide transformylase PurT C-terminal domain .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011054:Rudiment single hybrid motif
The ATP-grasp fold is one of several distinct ATP-binding folds.nd is found in enzymes that catalyze the formation of amide bonds.atalyzing the ATP-dependent ligation of a carboxylate-containing molecule to an amino or thiol group-containing molecule . This fold is found in many different enzyme families.ncluding various peptide synthetases.iotin carboxylase.ynapsin.uccinyl-CoA synthetase.yruvate phosphate dikinase.nd glutathione synthetase.mongst others . These enzymes contribute predominantly to macromolecular synthesis.sing ATP-hydrolysis to activate their substrates. The ATP-grasp fold shares functional and structural similarities with the PIPK (phosphatidylinositol phosphate kinase) and protein kinase superfamilies. The ATP-grasp domain consists of two subdomains with different alpha+beta folds.hich grasp the ATP molecule between them. Each subdomain provides a variable loop that forms part of the active site.ith regions from other domains also contributing to the active site.ven though these other domains are not conserved between the various ATP-grasp enzymes . This entry represents subdomain 2 found at the C-terminal end of the ATP-grasp domain (the N-terminal subdomain is represented by ().
  IPR013816:ATP-grasp fold, subdomain 2
IPR013537:ACC_central 
Evalue:-1e+125 
Location:819-1569IPR000022:Carboxyl_trans 
Evalue:-290.886047363281 
Location:1664-2223IPR005479:CPSase_L_D2 
Evalue:-58.5528411865234 
Location:291-475IPR005481:CPSase_L_chain 
Evalue:-57.6989707946777 
Location:117-240IPR005482:Biotin_carb_C 
Evalue:-49.6020584106445 
Location:507-614IPR000089:Biotin_lipoyl 
Evalue:-22.6575775146484 
Location:752-818
SequencesProtein: COA1_HUMAN (2346 aa)
mRNA: NM_198834 NM_198839
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01946
  Level 3 annotation:
    biotin carboxylase
  Level 2 annotation:
    Fatty acid biosynthesis
K01961
  Level 3 annotation:
    acetyl-CoA carboxylase
  Level 2 annotation:
    Pyruvate metabolism
    Propanoate metabolism
    Fatty acid biosynthesis
    Tetracycline biosynthesis
    Insulin signaling pathway
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 816 residues, 32516040-32518487Exon2: 47 residues, 32519985-32520122Exon3: 59 residues, 32528043-32528214Exon4: 53 residues, 32528877-32529032Exon5: 39 residues, 32542578-32542691Exon6: 61 residues, 32544135-32544313Exon7: 47 residues, 32552389-32552525Exon8: 34 residues, 32553565-32553662Exon9: 34 residues, 32556731-32556828Exon10: 42 residues, 32560403-32560524Exon11: 50 residues, 32561113-32561257Exon12: 39 residues, 32580900-32581011Exon13: 42 residues, 32582338-32582459Exon14: 34 residues, 32586717-32586815Exon15: 92 residues, 32592807-32593077Exon16: 51 residues, 32610313-32610460Exon17: 54 residues, 32612254-32612410Exon18: 70 residues, 32619329-32619533Exon19: 54 residues, 32622173-32622329Exon20: 74 residues, 32623143-32623359Exon21: 16 residues, 32624427-32624469Exon22: 17 residues, 32631194-32631239Exon23: 21 residues, 32631482-32631539Exon24: 38 residues, 32636791-32636899Exon25: 34 residues, 32637809-32637906Exon26: 50 residues, 32638683-32638827Exon27: 10 residues, 32641493-32641517Exon28: 41 residues, 32652757-32652876Exon29: 32 residues, 32654545-32654635Exon30: 40 residues, 32656025-32656139Exon31: 40 residues, 32657372-32657486Exon32: 43 residues, 32666002-32666127Exon33: 31 residues, 32671504-32671593Exon34: 35 residues, 32672981-32673082Exon35: 65 residues, 32674399-32674588Exon36: 51 residues, 32675616-32675763Exon37: 47 residues, 32676108-32676243Exon38: 52 residues, 32677854-32678005Exon39: 50 residues, 32679047-32679193Exon40: 29 residues, 32679629-32679711Exon41: 36 residues, 32683043-32683147Exon42: 52 residues, 32683924-32684075Exon43: 56 residues, 32688737-32688901Exon44: 56 residues, 32689246-32689408Exon45: 59 residues, 32690394-32690565Exon46: 72 residues, 32694700-32694910Exon47: 39 residues, 32701754-32701865Exon48: 37 residues, 32705196-32705303Exon49: 35 residues, 32706956-32707055Exon50: 29 residues, 32708038-32708120Exon51: 38 residues, 32708901-32709011Exon52: 48 residues, 32714280-32714419Exon53: 46 residues, 32715851-32715984Exon54: 86 residues, 32761225-32761478Exon55: 17 residues, 32770876-32770923Exon56: 45 residues, 32776322-32776452Exon57: 104 residues, 32796496-32796804Exon58: 41 residues, 32797998-32798116Exon59: 41 residues, 32800425-32800543Exon60: 185 residues, 32840464-32841015Exon61: 2 residues, -Jump to COA1_HUMANExon1: 816 residues, 32516040-32518487Exon2: 47 residues, 32519985-32520122Exon3: 59 residues, 32528043-32528214Exon4: 53 residues, 32528877-32529032Exon5: 39 residues, 32542578-32542691Exon6: 61 residues, 32544135-32544313Exon7: 47 residues, 32552389-32552525Exon8: 34 residues, 32553565-32553662Exon9: 34 residues, 32556731-32556828Exon10: 42 residues, 32560403-32560524Exon11: 50 residues, 32561113-32561257Exon12: 39 residues, 32580900-32581011Exon13: 42 residues, 32582338-32582459Exon14: 34 residues, 32586717-32586815Exon15: 92 residues, 32592807-32593077Exon16: 51 residues, 32610313-32610460Exon17: 54 residues, 32612254-32612410Exon18: 70 residues, 32619329-32619533Exon19: 54 residues, 32622173-32622329Exon20: 74 residues, 32623143-32623359Exon21: 16 residues, 32624427-32624469Exon22: 17 residues, 32631194-32631239Exon23: 21 residues, 32631482-32631539Exon24: 38 residues, 32636791-32636899Exon25: 34 residues, 32637809-32637906Exon26: 50 residues, 32638683-32638827Exon27: 10 residues, 32641493-32641517Exon28: 41 residues, 32652757-32652876Exon29: 32 residues, 32654545-32654635Exon30: 40 residues, 32656025-32656139Exon31: 40 residues, 32657372-32657486Exon32: 43 residues, 32666002-32666127Exon33: 31 residues, 32671504-32671593Exon34: 35 residues, 32672981-32673082Exon35: 65 residues, 32674399-32674588Exon36: 51 residues, 32675616-32675763Exon37: 47 residues, 32676108-32676243Exon38: 52 residues, 32677854-32678005Exon39: 50 residues, 32679047-32679193Exon40: 29 residues, 32679629-32679711Exon41: 36 residues, 32683043-32683147Exon42: 52 residues, 32683924-32684075Exon43: 56 residues, 32688737-32688901Exon44: 56 residues, 32689246-32689408Exon45: 59 residues, 32690394-32690565Exon46: 72 residues, 32694700-32694910Exon47: 39 residues, 32701754-32701865Exon48: 37 residues, 32705196-32705303Exon49: 35 residues, 32706956-32707055Exon50: 29 residues, 32708038-32708120Exon51: 38 residues, 32708901-32709011Exon52: 48 residues, 32714280-32714419Exon53: 46 residues, 32715851-32715984Exon54: 86 residues, 32761225-32761478Exon55: 17 residues, 32770876-32770923Exon56: 185 residues, 32840464-32841015Exon57: 2 residues, -Jump to COA1_HUMAN  
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