carB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

CarB

Synonyms

carbamoyl-phosphate synthase large subunit[1], B0033[2][1], Cap[2][1], PyrA[2][1], β chain[2][1], large chain[2][1], CarB[2][1] , cap, ECK0034, JW0031, pyrA, b0033

Product description

CarB[2][3];

Component of carbamoyl phosphate synthetase[2][3]

Carbamoyl phosphate synthase, ammonia, large subunit; tetramer of heterodimers[4]

EC number (for enzymes)

<protect></protect>

Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded from EcoCyc (v14.0)

complete

GO:0000166

nucleotide binding

PMID:15322282[5]

IPI: Inferred from Physical Interaction

F

Seeded from EcoCyc (v14.0)

Missing: with/from

GO:0000166

nucleotide binding

PMID:7648201[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005479

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

PMID:14718657[7]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005481

F

Seeded from EcoCyc (v14.0)

complete

Contributes to

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:14718657[7]

IDA: Inferred from Direct Assay

F

replaces obsoleteGO:0004086

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011761

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:4358555[8]

IDA: Inferred from Direct Assay

F

CarA

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013816

F

Seeded from EcoCyc (v14.0)

complete

GO:0004087

carbamoyl-phosphate synthase (ammonia) activity

PMID:3549732[9]

IDA: Inferred from Direct Assay

F

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013817

F

Seeded from EcoCyc (v14.0)

complete

GO:0046872

metal ion binding

PMID:229896[10]

IDA: Inferred from Direct Assay

F

complete

GO:0003824

catalytic activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016185

F

Seeded from EcoCyc (v14.0)

complete

GO:0019856

pyrimidine base biosynthetic process

PMID:1737023[11]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004086

carbamoyl-phosphate synthase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005480

F

Seeded from EcoCyc (v14.0)

complete

GO:0008652

cellular amino acid biosynthetic process

PMID:1737023[11]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004086

carbamoyl-phosphate synthase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005483

F

Seeded from EcoCyc (v14.0)

complete

Contributes to

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

PMID:1737023[11]

IGI: Inferred from Genetic Interaction

EcoliWiki:carA

F

complete

GO:0004086

carbamoyl-phosphate synthase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006275

F

Seeded from EcoCyc (v14.0)

complete

GO:0000166

nucleotide binding

PMID:10843852[12]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01210

F

Seeded from EcoCyc (v14.0)

complete

GO:0000166

nucleotide binding

PMID:7648201[6]

IDA: Inferred from Direct Assay

F

UMP (CHEBI:16695) & IMP (CHEBI:17202)

complete

GO:0004088

carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:6.3.5.5

F

Seeded from EcoCyc (v14.0)

complete

GO:0000166

nucleotide binding

PMID:15322282[5]

IPI: Inferred from Physical Interaction

F

IMP (CHEBI:17202)

Missing: with/from

GO:0005515

protein binding

PMID:4358555[8]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0016597

amino acid binding

PMID:7648201[6]

IDA: Inferred from Direct Assay

F

ornithine (CHEBI:18257)

complete

GO:0005524

ATP binding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01210

F

Seeded from EcoCyc (v14.0)

complete

GO:0016597

amino acid binding

PMID:10047492[13]

IPI: Inferred from Physical Interaction

F

ornithine (CHEBI:18257)

Missing: with/from

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005479

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011761

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013816

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013817

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR016185

F

Seeded from EcoCyc (v14.0)

complete

GO:0005524

ATP binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded from EcoCyc (v14.0)

complete

GO:0006221

pyrimidine nucleotide biosynthetic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01210

P

Seeded from EcoCyc (v14.0)

complete

GO:0006221

pyrimidine nucleotide biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0665

P

Seeded from EcoCyc (v14.0)

complete

GO:0006526

arginine biosynthetic process

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01210

P

Seeded from EcoCyc (v14.0)

complete

GO:0006526

arginine biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0055

P

Seeded from EcoCyc (v14.0)

complete

GO:0006807

nitrogen compound metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005480

P

Seeded from EcoCyc (v14.0)

complete

GO:0006807

nitrogen compound metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005483

P

Seeded from EcoCyc (v14.0)

complete

GO:0006807

nitrogen compound metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006275

P

Seeded from EcoCyc (v14.0)

complete

GO:0008152

metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005479

P

Seeded from EcoCyc (v14.0)

complete

GO:0008152

metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR005481

P

Seeded from EcoCyc (v14.0)

complete

GO:0008652

cellular amino acid biosynthetic process

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0028

P

Seeded from EcoCyc (v14.0)

complete

GO:0016597

amino acid binding

PMID:10047492[13]

IPI: Inferred from Physical Interaction

F

Seeded from EcoCyc (v14.0)

Missing: with/from

GO:0016597

amino acid binding

PMID:7648201[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0030145

manganese ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0464

F

Seeded from EcoCyc (v14.0)

complete

GO:0046872

metal ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc (v14.0)

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of carbamoyl phosphate synthetase

could be indirect

Protein

ahpF

PMID:16606699[14]

Experiment(s):EBI-1135376

Protein

zwf

PMID:16606699[14]

Experiment(s):EBI-1135376

Protein

groL

PMID:16606699[14]

Experiment(s):EBI-1135376

Protein

glpD

PMID:16606699[14]

Experiment(s):EBI-1135376

Protein

fimA

PMID:19402753[15]

LCMS(ID Probability):99.4

Protein

rpsJ

PMID:19402753[15]

LCMS(ID Probability):99.6

Protein

cysI

PMID:19402753[15]

MALDI(Z-score):26.028219

Protein

cysJ

PMID:19402753[15]

MALDI(Z-score):27.126484

Protein

CarA

PMID:4358555[8]

Small Molecule

ATP

PMID:14718657[7]

Small Molecule

Mg2+

PMID:229896[10]


</protect>

Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

<protect></protect>

Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM
ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA
DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGSGGG
IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM
GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP
RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA
LTKIRRELKD AGADRIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG
ITGLNADFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT
AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP
VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM AVEKAKEIGY PLVVRPSYVL
GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME
HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI
EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL
AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR
RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK
Length

1,073

Mol. Wt

117.842 kDa

pI

5.1 (calculated)

Extinction coefficient

68,190 - 69,940 (calc based on 31 Y, 4 W, and 14 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P00968

Domain

424..547

PF02787 Carbamoyl-phosphate synthetase large chain, oligomerisation domain

PMID:19920124[16]

Domain

956..1042

PF02142 MGS-like domain

PMID:19920124[16]

Domain

6..123

PF00289 Carbamoyl-phosphate synthase L chain, N-terminal domain

PMID:19920124[16]

Domain

558..669

PF00289 Carbamoyl-phosphate synthase L chain, N-terminal domain

PMID:19920124[16]

Domain

128..335

PF02786 Carbamoyl-phosphate synthase L chain, ATP binding domain

PMID:19920124[16]

Domain

674..877

PF02786 Carbamoyl-phosphate synthase L chain, ATP binding domain

PMID:19920124[16]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=carB taxon=562,83333 </beststructure>

Models

View models at:

</protect>

Structure figures

<protect>

</protect>

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

<protect></protect>

Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128027

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0000121

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P00968

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10135

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10135

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:944775

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000131

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:944775

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0133

Escherichia coli str. K-12 substr. MG1655

<protect></protect>

Notes

Links

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References

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

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 Thoden, JB et al. (2004) Long-range allosteric transitions in carbamoyl phosphate synthetase. Protein Sci. 13 2398-405 PubMed
  6. 6.0 6.1 6.2 6.3 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
  7. 7.0 7.1 7.2 Kothe, M & Powers-Lee, SG (2004) Nucleotide recognition in the ATP-grasp protein carbamoyl phosphate synthetase. Protein Sci. 13 466-75 PubMed
  8. 8.0 8.1 8.2 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
  9. 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
  10. 10.0 10.1 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
  11. 11.0 11.1 11.2 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
  12. 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
  13. 13.0 13.1 Delannay, S et al. (1999) Serine 948 and threonine 1042 are crucial residues for allosteric regulation of Escherichia coli carbamoylphosphate synthetase and illustrate coupling effects of activation and inhibition pathways. J. Mol. Biol. 286 1217-28 PubMed
  14. 14.0 14.1 14.2 14.3 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  15. 15.0 15.1 15.2 15.3 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  16. 16.0 16.1 16.2 16.3 16.4 16.5 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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