CPA2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004087 carbamoyl-phosphate synthase (ammonia) activity	EXP PMID:206535 Structure-function relationships in the arginine pathway car...	ACCEPT	Summary: Isolated Cpa2p (the heavy component) synthesises carbamoyl phosphate from ammonia, bicarbonate and 2 ATP (EC 6.3.4.16) without the small subunit. Reason: Direct experimental support for the large-subunit ligase activity. Supporting Evidence: PMID:206535 The large component catalyzed the synthesis of carbamoylphosphate from ammonia. PMID:206652 comprised two unequal subunits: a heavy subunit (mol. wt 80000) capable of catalysing synthesis of carbamoyl phosphate with ammonia as a nitrogen donor and a light subunit conferring upon the holoenzyme the ability to utilize glutamine.
GO:0004087 carbamoyl-phosphate synthase (ammonia) activity	EXP PMID:206652 Purification and properties of the arginine-specific carbamo...	ACCEPT	Summary: Isolated Cpa2p (the heavy component) synthesises carbamoyl phosphate from ammonia, bicarbonate and 2 ATP (EC 6.3.4.16) without the small subunit. Reason: Direct experimental support for the large-subunit ligase activity. Supporting Evidence: PMID:206535 The large component catalyzed the synthesis of carbamoylphosphate from ammonia. PMID:206652 comprised two unequal subunits: a heavy subunit (mol. wt 80000) capable of catalysing synthesis of carbamoyl phosphate with ammonia as a nitrogen donor and a light subunit conferring upon the holoenzyme the ability to utilize glutamine.
GO:0004087 carbamoyl-phosphate synthase (ammonia) activity	EXP PMID:5856369 The biosynthesis of carbamoyl phosphate in Saccharomyces cer...	ACCEPT	Summary: Isolated Cpa2p (the heavy component) synthesises carbamoyl phosphate from ammonia, bicarbonate and 2 ATP (EC 6.3.4.16) without the small subunit. Reason: Direct experimental support for the large-subunit ligase activity. Supporting Evidence: PMID:206535 The large component catalyzed the synthesis of carbamoylphosphate from ammonia. PMID:206652 comprised two unequal subunits: a heavy subunit (mol. wt 80000) capable of catalysing synthesis of carbamoyl phosphate with ammonia as a nitrogen donor and a light subunit conferring upon the holoenzyme the ability to utilize glutamine.
GO:0004087 carbamoyl-phosphate synthase (ammonia) activity	IBA GO_REF:0000033	ACCEPT	Summary: Ammonia-dependent CPSase is the intrinsic activity of CarB-family large subunits; consistent with experiment. Reason: Phylogenetic and experimental agreement. Supporting Evidence: PMID:206535 The large component catalyzed the synthesis of carbamoylphosphate from ammonia.
GO:0004087 carbamoyl-phosphate synthase (ammonia) activity	IEA GO_REF:0000120	ACCEPT	Summary: EC 6.3.4.16 mapping; correct. Reason: Consistent with experimental data. Supporting Evidence: PMID:206535 The large component catalyzed the synthesis of carbamoylphosphate from ammonia.
GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	EXP PMID:206535 Structure-function relationships in the arginine pathway car...	ACCEPT	Summary: Cpa2p carries out all synthetase chemistry of the glutamine-dependent reaction (EC 6.3.5.5) once Cpa1p supplies ammonia; strictly the activity is of the heterodimer, to which Cpa2p contributes most of the catalysis. Reason: Experimental support; curator annotation retained. Supporting Evidence: PMID:8626695 with a 45-kDa CPA1 subunit binding and cleaving glutamine, and a 124-kDa CPA2 subunit accepting the ammonia moiety cleaved from glutamine, binding all of the remaining substrates and carrying out all of the other catalytic events. PMID:206535 indicated that binding of glutamine to a site located on the small component was followed by transfer of its amide nitrogen to the ammonia site on the heavy component.
GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	EXP PMID:206652 Purification and properties of the arginine-specific carbamo...	ACCEPT	Summary: Cpa2p carries out all synthetase chemistry of the glutamine-dependent reaction (EC 6.3.5.5) once Cpa1p supplies ammonia; strictly the activity is of the heterodimer, to which Cpa2p contributes most of the catalysis. Reason: Experimental support; curator annotation retained. Supporting Evidence: PMID:8626695 with a 45-kDa CPA1 subunit binding and cleaving glutamine, and a 124-kDa CPA2 subunit accepting the ammonia moiety cleaved from glutamine, binding all of the remaining substrates and carrying out all of the other catalytic events. PMID:206535 indicated that binding of glutamine to a site located on the small component was followed by transfer of its amide nitrogen to the ammonia site on the heavy component.
GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	EXP PMID:5856369 The biosynthesis of carbamoyl phosphate in Saccharomyces cer...	ACCEPT	Summary: Cpa2p carries out all synthetase chemistry of the glutamine-dependent reaction (EC 6.3.5.5) once Cpa1p supplies ammonia; strictly the activity is of the heterodimer, to which Cpa2p contributes most of the catalysis. Reason: Experimental support; curator annotation retained. Supporting Evidence: PMID:8626695 with a 45-kDa CPA1 subunit binding and cleaving glutamine, and a 124-kDa CPA2 subunit accepting the ammonia moiety cleaved from glutamine, binding all of the remaining substrates and carrying out all of the other catalytic events. PMID:206535 indicated that binding of glutamine to a site located on the small component was followed by transfer of its amide nitrogen to the ammonia site on the heavy component.
GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	IDA PMID:8626695 Requirement for the carboxyl-terminal domain of Saccharomyce...	ACCEPT	Summary: contributes_to glutamine-dependent CPSase activity of the heterodimer; C-terminal domain of Cpa2p is required for catalysis. Reason: Direct experimental support. Supporting Evidence: PMID:8626695 with a 45-kDa CPA1 subunit binding and cleaving glutamine, and a 124-kDa CPA2 subunit accepting the ammonia moiety cleaved from glutamine, binding all of the remaining substrates and carrying out all of the other catalytic events. PMID:8626695 essentially all of the carboxyl-terminal domain of CPA2 is required for catalytic function
GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	IEA GO_REF:0000120	ACCEPT	Summary: EC 6.3.5.5 mapping; correct for the complex to which Cpa2p contributes. Reason: Consistent with experimental data. Supporting Evidence: PMID:8626695 with a 45-kDa CPA1 subunit binding and cleaving glutamine, and a 124-kDa CPA2 subunit accepting the ammonia moiety cleaved from glutamine, binding all of the remaining substrates and carrying out all of the other catalytic events.
GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	IMP PMID:6358221 Yeast carbamyl phosphate synthetase. Structure of the yeast ...	ACCEPT	Summary: Cloning/sequencing of CPA2 (by complementation-based identification) establishing it as the large CPSase subunit gene; contributes_to. Reason: Supports the subunit assignment. Supporting Evidence: PMID:6358221 A cloned fragment of yeast chromosomal DNA carrying the gene CPA2 coding for the large subunit of arginine-specific carbamyl phosphate synthetase has been sequenced.
GO:0004088 carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	RCA GO_REF:0000123	ACCEPT	Summary: YeastPathways CPSase step of arginine biosynthesis; correct. Reason: Pathway assignment agrees with enzymology. Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
GO:0005524 ATP binding	IEA GO_REF:0000002	ACCEPT	Summary: ATP substrate binding is intrinsic to the core catalytic reaction. Reason: This experimentally established or conserved substrate/cofactor interaction is part of the core enzyme mechanism. Being required for catalysis or already implied by a catalytic activity does not make it a peripheral function. Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt The large subunit is composed of 2 ATP-grasp domains that are
GO:0005737 cytoplasm	EXP PMID:14562095 Global analysis of protein localization in budding yeast.	MODIFY	Summary: The cytoplasm annotation is compatible with the more specific supported cellular compartment. Reason: Cytoplasm includes the relevant organelle/cytosolic compartment in GO. Refine this broad true term to cytosol, supported by the combined localization evidence; do not call the broad term a contradictory location or infer tag interference without examining the original images. Proposed replacements: cytosol Supporting Evidence: PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the file:yeast/CPA2/CPA2-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269\|PubMed:14562095, PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the "soluble" fraction of the cell.
GO:0005737 cytoplasm	EXP PMID:200419 Change in location of ornithine carbamoyltransferase and car...	MODIFY	Summary: The cytoplasm annotation is compatible with the more specific supported cellular compartment. Reason: Cytoplasm includes the relevant organelle/cytosolic compartment in GO. Refine this broad true term to cytosol, supported by the combined localization evidence; do not call the broad term a contradictory location or infer tag interference without examining the original images. Proposed replacements: cytosol Supporting Evidence: PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the file:yeast/CPA2/CPA2-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269\|PubMed:14562095, PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the "soluble" fraction of the cell.
GO:0005737 cytoplasm	EXP PMID:205532 Arginine metabolism in Saccharomyces cerevisiae: subcellular...	MODIFY	Summary: The cytoplasm annotation is compatible with the more specific supported cellular compartment. Reason: Cytoplasm includes the relevant organelle/cytosolic compartment in GO. Refine this broad true term to cytosol, supported by the combined localization evidence; do not call the broad term a contradictory location or infer tag interference without examining the original images. Proposed replacements: cytosol Supporting Evidence: PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the file:yeast/CPA2/CPA2-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269\|PubMed:14562095, PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the "soluble" fraction of the cell.
GO:0005737 cytoplasm	IBA GO_REF:0000033	MODIFY	Summary: The cytoplasm annotation is compatible with the more specific supported cellular compartment. Reason: Cytoplasm includes the relevant organelle/cytosolic compartment in GO. Refine this broad true term to cytosol, supported by the combined localization evidence; do not call the broad term a contradictory location or infer tag interference without examining the original images. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000150222 SUPPORTS TRANSFER The broad inherited cellular location remains true. Refinement uses target-specific localization and does not allege faulty ancestral placement or a change from cytoplasm to a non-cytoplasmic organelle. Proposed replacements: cytosol Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269\|PubMed:14562095, PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the "soluble" fraction of the cell.
GO:0005737 cytoplasm	IDA PMID:206535 Structure-function relationships in the arginine pathway car...	MODIFY	Summary: The cytoplasm annotation is compatible with the more specific supported cellular compartment. Reason: Cytoplasm includes the relevant organelle/cytosolic compartment in GO. Refine this broad true term to cytosol, supported by the combined localization evidence; do not call the broad term a contradictory location or infer tag interference without examining the original images. Proposed replacements: cytosol Supporting Evidence: PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the "soluble" fraction of the cell.
GO:0005737 cytoplasm	IEA GO_REF:0000120	MODIFY	Summary: The cytoplasm annotation is compatible with the more specific supported cellular compartment. Reason: Cytoplasm includes the relevant organelle/cytosolic compartment in GO. Refine this broad true term to cytosol, supported by the combined localization evidence; do not call the broad term a contradictory location or infer tag interference without examining the original images. Proposed replacements: cytosol Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269\|PubMed:14562095, PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the "soluble" fraction of the cell.
GO:0005829 cytosol	RCA GO_REF:0000123	ACCEPT	Summary: Soluble (cytosolic) location of CPSase A in S. cerevisiae; correct. Reason: Consistent with fractionation data. Supporting Evidence: PMID:205532 arginine pathway-specific carbamoylphosphate synthetase, ornithine carbamoyltransferase, argininosuccinate synthetase, and argininosuccinate lyase, and the two first catabolic enzymes, arginase and ornithine aminotransferase, were in the
GO:0005951 carbamoyl-phosphate synthase complex	IDA PMID:206535 Structure-function relationships in the arginine pathway car...	ACCEPT	Summary: Cpa2p is the large subunit of the CPSase A heterodimer. Reason: Direct experimental support. Supporting Evidence: PMID:206535 The enzyme is an aggregate consisting of two protein components, coded for by the unlinked genes cpaI and cpaII.
GO:0005951 carbamoyl-phosphate synthase complex	IPI PMID:206535 Structure-function relationships in the arginine pathway car...	ACCEPT	Summary: Physical association of Cpa2p with Cpa1p; Cpa1p also stimulates Cpa2p Vmax even with ammonia as substrate. Reason: Direct experimental support. Supporting Evidence: PMID:206535 The enzyme is an aggregate consisting of two protein components, coded for by the unlinked genes cpaI and cpaII. PMID:8626695 interaction with CPA1 led to an increase in the Vmax of CPA2 in crude extracts.
GO:0006221 pyrimidine nucleotide biosynthetic process	IDA PMID:206535 Structure-function relationships in the arginine pathway car...	KEEP AS NON CORE	Summary: Carbamoyl phosphate from CPSase A can feed the single cellular pool also used by the pyrimidine pathway, but the physiological role of Cpa2p is arginine biosynthesis; the pyrimidine-pathway CPSase is URA2. Reason: Deferred to curator (full text not available); secondary role. Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt appear to contribute to the formation of a single cellular pool of
GO:0006526 L-arginine biosynthetic process	IBA GO_REF:0000033	ACCEPT	Summary: CPSase A supplies carbamoyl phosphate for citrulline synthesis in arginine biosynthesis. Reason: Core pathway. Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
GO:0006526 L-arginine biosynthetic process	IDA PMID:206535 Structure-function relationships in the arginine pathway car...	ACCEPT	Summary: Arginine-pathway CPSase characterised biochemically. Reason: Core pathway. Supporting Evidence: PMID:206535 The enzyme is an aggregate consisting of two protein components, coded for by the unlinked genes cpaI and cpaII.
GO:0006526 L-arginine biosynthetic process	IEA GO_REF:0000120	ACCEPT	Summary: Correct pathway mapping. Reason: Core pathway. Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
GO:0006526 L-arginine biosynthetic process	IMP PMID:8626695 Requirement for the carboxyl-terminal domain of Saccharomyce...	ACCEPT	Summary: C-terminal deletions of Cpa2p abolish catalytic function; mutant analysis supports the arginine pathway role. Reason: Core pathway. Supporting Evidence: PMID:8626695 essentially all of the carboxyl-terminal domain of CPA2 is required for catalytic function
GO:0006526 L-arginine biosynthetic process	RCA GO_REF:0000123	ACCEPT	Summary: YeastPathways arginine biosynthesis assignment; correct. Reason: Core pathway. Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
GO:0046872 metal ion binding	IEA GO_REF:0000002	MODIFY	Summary: The CPS synthetase domains bind divalent magnesium or manganese ions. Reason: Refine metal ion binding to magnesium ion binding and manganese ion binding, both specified by the curated PROSITE/ProRule-supported cofactor assignment. These are catalytic cofactors, not peripheral functions; the assignment is a domain-based inference rather than a new target-specific stoichiometric binding measurement. Proposed replacements: magnesium ion binding manganese ion binding Supporting Evidence: file:yeast/CPA2/CPA2-uniprot.txt Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit.

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

SGD

SGD gene description for CPA2 (yeast)

📚 Additional Documentation

Notes

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