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ECOLI:CARB

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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 Extension 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

Notes

References

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

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