SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0MCCA_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMCCC1
DescriptionMethylcrotonoyl-coa carboxylase alpha chain, mitochondrial precursor (ec 6.4.1.4) (3-methylcrotonyl-coa carboxylase 1) (mccase alpha subunit) (3-methylcrotonyl-coa:carbon dioxide ligase alpha subunit) (3-methylcrotonyl-coa carboxylase biotin-containing subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005759 mitochondrial matrix (NAS)
0009374 biotin binding (NAS)
0004485 methylcrotonoyl-CoA carboxylase activity (NAS)
0006768 biotin metabolism (NAS)
0006552 leucine catabolism (NAS)

Warning: fopen(/home/kongl/syndb/www/temp/182757290.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
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 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 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 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
IPR005479:CPSase_L_D2 
Evalue:-101 
Location:163-376IPR005481:CPSase_L_chain 
Evalue:-51.5528411865234 
Location:48-160IPR005482:Biotin_carb_C 
Evalue:-44.6989707946777 
Location:383-490IPR000089:Biotin_lipoyl 
Evalue:-18.4202156066895 
Location:651-714
SequencesProtein: MCCA_HUMAN (725 aa)
mRNA: NM_020166
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK01968
  Level 3 annotation:
    3-methylcrotonyl-CoA carboxylase alpha subunit
  Level 2 annotation:
    Valine
     leucine and isoleucine degradation
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 116 residues, 184215701-184216048Exon2: 26 residues, 184217747-184217819Exon3: 38 residues, 184220611-184220719Exon4: 48 residues, 184222898-184223036Exon5: 18 residues, 184226236-184226286Exon6: 31 residues, 184234472-184234559Exon7: 74 residues, 184237699-184237916Exon8: 38 residues, 184239507-184239617Exon9: 63 residues, 184242048-184242232Exon10: 44 residues, 184245894-184246022Exon11: 29 residues, 184252640-184252722Exon12: 39 residues, 184257792-184257904Exon13: 42 residues, 184271480-184271602Exon14: 51 residues, 184271691-184271839Exon15: 42 residues, 184272847-184272969Exon16: 34 residues, 184287174-184287270Exon17: 47 residues, 184292890-184293027Exon18: 17 residues, 184295040-184295087Exon19: 75 residues, 184299833-184300054Exon20: 2 residues, -Jump to MCCA_HUMAN  
Tune and view alternative isoforms