ECOLI:CARB

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	carB (synonyms: pyrA)
Protein Name(s)	Carbamoyl-phosphate synthase large chain Carbamoyl-phosphate synthetase ammonia chain
External Links
UniProt	P00968
EMBL	J01597 V01500 U00096 AP009048
PIR	A01198
RefSeq	NP_414574.1 YP_488339.1
PDB	1A9X 1BXR 1C30 1C3O 1CE8 1CS0 1JDB 1KEE 1M6V 1T36
PDBsum	1A9X 1BXR 1C30 1C3O 1CE8 1CS0 1JDB 1KEE 1M6V 1T36
ProteinModelPortal	P00968
SMR	P00968
DIP	DIP-1025N
IntAct	P00968
MINT	MINT-1255866
STRING	511145.b0033
PaxDb	P00968
PRIDE	P00968
EnsemblBacteria	AAC73144 BAB96602
GeneID	12930732 944775
KEGG	ecj:Y75_p0033 eco:b0033
PATRIC	32115159
EchoBASE	EB0133
EcoGene	EG10135
eggNOG	COG0458
HOGENOM	HOG000234582
InParanoid	P00968
KO	K01955
OMA	AVFPFNK
OrthoDB	EOG6J1DC6
PhylomeDB	P00968
BioCyc	EcoCyc:CARBPSYN-LARGE ECOL316407:JW0031-MONOMER MetaCyc:CARBPSYN-LARGE
SABIO-RK	P00968
UniPathway	UPA00068 UPA00070
EvolutionaryTrace	P00968
PRO	PR:P00968
Proteomes	UP000000318 UP000000625
Genevestigator	P00968
GO	GO:0005951 GO:0016597 GO:0005524 GO:0004087 GO:0004088 GO:0046872 GO:0000166 GO:0044205 GO:0006526 GO:0042710 GO:0008652 GO:0019856
Gene3D	1.10.1030.10 3.30.1490.20 3.30.470.20 3.40.50.1380 3.40.50.20
HAMAP	MF_01210_A MF_01210_B
InterPro	IPR011761 IPR013815 IPR013816 IPR006275 IPR005481 IPR005480 IPR005479 IPR005483 IPR011607 IPR016185
Pfam	PF00289 PF02786 PF02787 PF02142
PRINTS	PR00098
SMART	SM01096 SM00851
SUPFAM	SSF48108 SSF52335 SSF52440
TIGRFAMs	TIGR01369
PROSITE	PS50975 PS00866 PS00867

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0042710	biofilm formation	PMID:22359582^[1]	ECO:0000315			P	Figure 1. Congo red binding tests show that carB deletion mutant is unable to produce curli, fibers that are important components of biofilm matrix.	complete CACAO 5383
involved_in	GO:0006807	nitrogen compound metabolic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10134 EcoGene:EG10135 FB:FBgn0003189 PANTHER:PTN000150222 PomBase:SPAC22G7.06c PomBase:SPBC215.08c PomBase:SPBC56F2.09c RGD:1588606 RGD:2395 SGD:S000003666 SGD:S000003870 SGD:S000005829 TAIR:locus:2092369 UniProtKB:O93937 UniProtKB:P27708 UniProtKB:P31327 UniProtKB:P38100 WB:WBGene00004259 ZFIN:ZDB-GENE-021030-4 ZFIN:ZDB-GENE-081105-17 dictyBase:DDB_G0276335	P	Seeded From UniProt	complete
involved_in	GO:0006541	glutamine metabolic process	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003189 PANTHER:PTN000150223 PomBase:SPAC22G7.06c RGD:1588606 SGD:S000003666 dictyBase:DDB_G0276335	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10134 EcoGene:EG10135 EcoGene:EG10805 MGI:MGI:891996 PANTHER:PTN000150222 RGD:1588606 RGD:2395 SGD:S000003666 SGD:S000003870 SGD:S000005829 TAIR:locus:2019302 TAIR:locus:2092369 UniProtKB:P27708 UniProtKB:P31327 UniProtKB:P9WIT7 UniProtKB:Q9LVW7	C	Seeded From UniProt	complete
contributes_to	GO:0004088	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	PMID:21873635^[2]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10135 PANTHER:PTN000150223 SGD:S000003870	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	PMID:229896^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0019856	pyrimidine nucleobase biosynthetic process	PMID:1737023^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016597	amino acid binding	PMID:7648201^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0008652	cellular amino acid biosynthetic process	PMID:1737023^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:14718657^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004087	carbamoyl-phosphate synthase (ammonia) activity	PMID:3549732^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	PMID:10843852^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	PMID:7648201^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005951	carbamoyl-phosphate synthase complex	PMID:4358555^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:1737023^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005479 InterPro:IPR011761	F	Seeded From UniProt	complete
involved_in	GO:0006807	nitrogen compound metabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005483 InterPro:IPR006275	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR011761	F	Seeded From UniProt	complete
enables	GO:0004088	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.3.5.5	F	Seeded From UniProt	complete
involved_in	GO:0006221	pyrimidine nucleotide biosynthetic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101215	P	Seeded From UniProt	complete
involved_in	GO:0006526	arginine biosynthetic process	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101215	P	Seeded From UniProt	complete
enables	GO:0004088	carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101215	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000101215	F	Seeded From UniProt	complete
involved_in	GO:0006221	pyrimidine nucleotide biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0665	P	Seeded From UniProt	complete
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
involved_in	GO:0008652	cellular amino acid biosynthetic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0028	P	Seeded From UniProt	complete
involved_in	GO:0006526	arginine biosynthetic process	GO_REF:0000037 GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0055 UniPathway:UPA00068	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0044205	'de novo' UMP biosynthetic process	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00070	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Garavaglia, M et al. (2012) The pyrimidine nucleotide biosynthetic pathway modulates production of biofilm determinants in Escherichia coli. PLoS ONE 7 e31252 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Raushel, FM et al. (1979) Paramagnetic probes for carbamoyl-phosphate synthetase: metal ion binding studies and preparation of nitroxide spin-labeled derivatives. Biochemistry 18 5562-6 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Guillou, F et al. (1992) Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu841 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit. Biochemistry 31 1656-64 PubMed GONUTS page
↑ ^5.0 ^5.1 Mareya, SM & Raushel, FM (1995) Mapping the structural domains of E. coli carbamoyl phosphate synthetase using limited proteolysis. Bioorg. Med. Chem. 3 525-32 PubMed GONUTS page
↑ Kothe, M & Powers-Lee, SG (2004) Nucleotide recognition in the ATP-grasp protein carbamoyl phosphate synthetase. Protein Sci. 13 466-75 PubMed GONUTS page
↑ Rubino, SD et al. (1987) In vivo synthesis of carbamyl phosphate from NH3 by the large subunit of Escherichia coli carbamyl phosphate synthetase. J. Biol. Chem. 262 4382-6 PubMed GONUTS page
↑ Fresquet, V et al. (2000) Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals. J. Mol. Biol. 299 979-91 PubMed GONUTS page
↑ Trotta, PP et al. (1974) Reversible dissociation of the monomer of glutamine-dependent carbamyl phosphate synthetase into catalytically active heavy and light subunits. J. Biol. Chem. 249 492-9 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:22359582-1] Garavaglia, M et al. (2012) The pyrimidine nucleotide biosynthetic pathway modulates production of biofilm determinants in Escherichia coli. PLoS ONE 7 e31252 PubMed GONUTS page

[PMID:21873635-2] 2.0 ^2.1 ^2.2 ^2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:229896-3] Raushel, FM et al. (1979) Paramagnetic probes for carbamoyl-phosphate synthetase: metal ion binding studies and preparation of nitroxide spin-labeled derivatives. Biochemistry 18 5562-6 PubMed GONUTS page

[PMID:1737023-4] 4.0 ^4.1 ^4.2 Guillou, F et al. (1992) Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu841 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit. Biochemistry 31 1656-64 PubMed GONUTS page

[PMID:7648201-5] 5.0 ^5.1 Mareya, SM & Raushel, FM (1995) Mapping the structural domains of E. coli carbamoyl phosphate synthetase using limited proteolysis. Bioorg. Med. Chem. 3 525-32 PubMed GONUTS page

[PMID:14718657-6] Kothe, M & Powers-Lee, SG (2004) Nucleotide recognition in the ATP-grasp protein carbamoyl phosphate synthetase. Protein Sci. 13 466-75 PubMed GONUTS page

[PMID:3549732-7] Rubino, SD et al. (1987) In vivo synthesis of carbamyl phosphate from NH3 by the large subunit of Escherichia coli carbamyl phosphate synthetase. J. Biol. Chem. 262 4382-6 PubMed GONUTS page

[PMID:10843852-8] Fresquet, V et al. (2000) Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals. J. Mol. Biol. 299 979-91 PubMed GONUTS page

[PMID:4358555-9] Trotta, PP et al. (1974) Reversible dissociation of the monomer of glutamine-dependent carbamyl phosphate synthetase into catalytically active heavy and light subunits. J. Biol. Chem. 249 492-9 PubMed GONUTS page

[PMID:18304323-10] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-11] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

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ECOLI:CARB

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