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P00968

- CARB_ECOLI

UniProt

P00968 - CARB_ECOLI

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Protein
Carbamoyl-phosphate synthase large chain
Gene
carB, pyrA, b0033, JW0031
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.UniRule annotation

Cofactori

Binds 4 manganese ions per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi285 – 2851Manganese 1
Metal bindingi299 – 2991Manganese 1
Metal bindingi299 – 2991Manganese 2
Metal bindingi301 – 3011Manganese 2
Metal bindingi829 – 8291Manganese 3
Metal bindingi841 – 8411Manganese 3
Metal bindingi841 – 8411Manganese 4 By similarity
Metal bindingi843 – 8431Manganese 4 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATP By similarity
Add
BLAST
Nucleotide bindingi705 – 76258ATP By similarity
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: EcoCyc
  2. amino acid binding Source: EcoliWiki
  3. carbamoyl-phosphate synthase (ammonia) activity Source: EcoliWiki
  4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-HAMAP
  5. magnesium ion binding Source: UniProtKB-HAMAP
  6. manganese ion binding Source: UniProtKB-HAMAP
  7. metal ion binding Source: EcoliWiki
  8. nucleotide binding Source: EcoliWiki
  9. protein binding Source: IntAct

GO - Biological processi

  1. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  2. arginine biosynthetic process Source: UniProtKB-HAMAP
  3. biofilm formation Source: CACAO
  4. cellular amino acid biosynthetic process Source: EcoliWiki
  5. pyrimidine nucleobase biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CARBPSYN-LARGE.
ECOL316407:JW0031-MONOMER.
MetaCyc:CARBPSYN-LARGE.
SABIO-RKP00968.
UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase large chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:carB
Synonyms:pyrA
Ordered Locus Names:b0033, JW0031
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10135. carB.

Subcellular locationi

GO - Cellular componenti

  1. carbamoyl-phosphate synthase complex Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10731072Carbamoyl-phosphate synthase large chainUniRule annotation
PRO_0000145004Add
BLAST

Proteomic databases

PaxDbiP00968.
PRIDEiP00968.

Expressioni

Gene expression databases

GenevestigatoriP00968.

Interactioni

Subunit structurei

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4.

Binary interactionsi

WithEntry#Exp.IntActNotes
carAP0A6F111EBI-546118,EBI-546107

Protein-protein interaction databases

DIPiDIP-1025N.
IntActiP00968. 13 interactions.
MINTiMINT-1255866.
STRINGi511145.b0033.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135
Helixi25 – 4016
Beta strandi43 – 475
Helixi54 – 563
Helixi58 – 603
Beta strandi61 – 655
Helixi71 – 8111
Beta strandi84 – 874
Beta strandi89 – 913
Helixi92 – 10413
Helixi107 – 1115
Helixi120 – 1278
Helixi129 – 13810
Beta strandi145 – 1517
Helixi152 – 16211
Beta strandi164 – 1707
Turni175 – 1784
Beta strandi180 – 1845
Helixi185 – 19814
Beta strandi204 – 2085
Beta strandi213 – 22210
Beta strandi228 – 23811
Helixi244 – 2463
Beta strandi249 – 2524
Helixi258 – 27518
Beta strandi279 – 28810
Turni290 – 2923
Beta strandi295 – 3039
Helixi306 – 31510
Helixi319 – 3279
Helixi332 – 3343
Turni338 – 3425
Beta strandi344 – 3463
Beta strandi353 – 3619
Helixi364 – 3663
Beta strandi382 – 3909
Helixi391 – 40111
Beta strandi402 – 4054
Beta strandi407 – 4093
Helixi420 – 42910
Helixi435 – 44410
Helixi449 – 4568
Helixi460 – 47920
Helixi481 – 4833
Helixi486 – 4949
Helixi499 – 5057
Helixi510 – 51910
Beta strandi525 – 5284
Beta strandi541 – 5477
Beta strandi557 – 5593
Beta strandi561 – 5655
Helixi576 – 59116
Beta strandi595 – 5995
Helixi606 – 6083
Beta strandi612 – 6176
Helixi623 – 63311
Beta strandi636 – 6394
Beta strandi641 – 6433
Helixi645 – 6484
Helixi651 – 6566
Beta strandi661 – 6644
Helixi666 – 6738
Helixi675 – 68511
Beta strandi692 – 6943
Helixi698 – 70811
Beta strandi710 – 7156
Turni721 – 7244
Beta strandi725 – 7284
Helixi731 – 74010
Beta strandi751 – 7544
Beta strandi760 – 7689
Beta strandi773 – 78311
Helixi789 – 7913
Beta strandi794 – 7974
Beta strandi799 – 8013
Helixi803 – 81917
Beta strandi824 – 8329
Beta strandi837 – 8437
Helixi850 – 8578
Helixi861 – 8699
Helixi874 – 8774
Beta strandi886 – 8949
Helixi896 – 8994
Beta strandi915 – 9239
Helixi924 – 93411
Beta strandi941 – 9488
Helixi951 – 9544
Helixi957 – 96610
Beta strandi970 – 9734
Helixi975 – 9828
Turni983 – 9853
Beta strandi989 – 9924
Turni994 – 9963
Beta strandi998 – 10003
Helixi1001 – 10077
Beta strandi1011 – 10155
Helixi1020 – 10256
Helixi1027 – 10359
Beta strandi1039 – 10435
Helixi1044 – 105411
Turni1058 – 10603
Helixi1065 – 10706

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9XX-ray1.80A/C/E/G1-1073[»]
1BXRX-ray2.10A/C/E/G1-1073[»]
1C30X-ray2.00A/C/E/G1-1073[»]
1C3OX-ray2.10A/C/E/G1-1073[»]
1CE8X-ray2.10A/C/E/G1-1073[»]
1CS0X-ray2.00A/C/E/G1-1073[»]
1JDBX-ray2.10B/E/H/K1-1073[»]
1KEEX-ray2.10A/C/E/G1-1073[»]
1M6VX-ray2.10A/C/E/G1-1073[»]
1T36X-ray2.10A/C/E/G1-1073[»]
ProteinModelPortaliP00968.
SMRiP00968. Positions 1-1073.

Miscellaneous databases

EvolutionaryTraceiP00968.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 328196ATP-grasp 1
Add
BLAST
Domaini679 – 870192ATP-grasp 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 403402Carboxyphosphate synthetic domainUniRule annotation
Add
BLAST
Regioni404 – 553150Oligomerization domainUniRule annotation
Add
BLAST
Regioni554 – 936383Carbamoyl phosphate synthetic domainUniRule annotation
Add
BLAST
Regioni937 – 1073137Allosteric domainUniRule annotation
Add
BLAST

Sequence similaritiesi

Belongs to the CarB family.
Contains 2 ATP-grasp domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0458.
HOGENOMiHOG000234582.
KOiK01955.
OMAiGSDRIWY.
OrthoDBiEOG6J1DC6.
PhylomeDBiP00968.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
HAMAPiMF_01210_A. CPSase_L_chain_A.
MF_01210_B. CPSase_L_chain_B.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00968-1 [UniParc]FASTAAdd to Basket

« Hide

MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN     50
PATIMTDPEM ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL 100
ELERQGVLEE FGVTMIGATA DAIDKAEDRR RFDVAMKKIG LETARSGIAH 150
TMEEALAVAA DVGFPCIIRP SFTMGGSGGG IAYNREEFEE ICARGLDLSP 200
TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM GIHTGDSITV 250
APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM 300
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP 350
SIDYVVTKIP RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR 400
GLEVGATGFD PKVSLDDPEA LTKIRRELKD AGADRIWYIA DAFRAGLSVD 450
GVFNLTNIDR WFLVQIEELV RLEEKVAEVG ITGLNADFLR QLKRKGFADA 500
RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT AYMYSTYEEE 550
CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN 600
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL 650
ARALEAAGVP VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM 700
AVEKAKEIGY PLVVRPSYVL GGRAMEIVYD EADLRRYFQT AVSVSNDAPV 750
LLDHFLDDAV EVDVDAICDG EMVLIGGIME HIEQAGVHSG DSACSLPAYT 800
LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI EVNPRAARTV 850
PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF 900
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR 950
EGDKERVVDL AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH 1000
IQDRIKNGEY TYIINTTSGR RAIEDSRVIR RSALQYKVHY DTTLNGGFAT 1050
AMALNADATE KVISVQEMHA QIK 1073
Length:1,073
Mass (Da):117,842
Last modified:January 23, 2007 - v2
Checksum:iA09D019CBDFF8D2B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01597 Genomic DNA. Translation: AAA23539.1.
V01500 Genomic DNA. Translation: CAA24744.1.
U00096 Genomic DNA. Translation: AAC73144.1.
AP009048 Genomic DNA. Translation: BAB96602.1.
PIRiA01198. SYECCP.
RefSeqiNP_414574.1. NC_000913.3.
YP_488339.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73144; AAC73144; b0033.
BAB96602; BAB96602; BAB96602.
GeneIDi12930732.
944775.
KEGGiecj:Y75_p0033.
eco:b0033.
PATRICi32115159. VBIEscCol129921_0031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J01597 Genomic DNA. Translation: AAA23539.1 .
V01500 Genomic DNA. Translation: CAA24744.1 .
U00096 Genomic DNA. Translation: AAC73144.1 .
AP009048 Genomic DNA. Translation: BAB96602.1 .
PIRi A01198. SYECCP.
RefSeqi NP_414574.1. NC_000913.3.
YP_488339.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A9X X-ray 1.80 A/C/E/G 1-1073 [» ]
1BXR X-ray 2.10 A/C/E/G 1-1073 [» ]
1C30 X-ray 2.00 A/C/E/G 1-1073 [» ]
1C3O X-ray 2.10 A/C/E/G 1-1073 [» ]
1CE8 X-ray 2.10 A/C/E/G 1-1073 [» ]
1CS0 X-ray 2.00 A/C/E/G 1-1073 [» ]
1JDB X-ray 2.10 B/E/H/K 1-1073 [» ]
1KEE X-ray 2.10 A/C/E/G 1-1073 [» ]
1M6V X-ray 2.10 A/C/E/G 1-1073 [» ]
1T36 X-ray 2.10 A/C/E/G 1-1073 [» ]
ProteinModelPortali P00968.
SMRi P00968. Positions 1-1073.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-1025N.
IntActi P00968. 13 interactions.
MINTi MINT-1255866.
STRINGi 511145.b0033.

Proteomic databases

PaxDbi P00968.
PRIDEi P00968.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73144 ; AAC73144 ; b0033 .
BAB96602 ; BAB96602 ; BAB96602 .
GeneIDi 12930732.
944775.
KEGGi ecj:Y75_p0033.
eco:b0033.
PATRICi 32115159. VBIEscCol129921_0031.

Organism-specific databases

EchoBASEi EB0133.
EcoGenei EG10135. carB.

Phylogenomic databases

eggNOGi COG0458.
HOGENOMi HOG000234582.
KOi K01955.
OMAi GSDRIWY.
OrthoDBi EOG6J1DC6.
PhylomeDBi P00968.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00171 .
UPA00070 ; UER00115 .
BioCyci EcoCyc:CARBPSYN-LARGE.
ECOL316407:JW0031-MONOMER.
MetaCyc:CARBPSYN-LARGE.
SABIO-RK P00968.

Miscellaneous databases

EvolutionaryTracei P00968.
PROi P00968.

Gene expression databases

Genevestigatori P00968.

Family and domain databases

Gene3Di 1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
HAMAPi MF_01210_A. CPSase_L_chain_A.
MF_01210_B. CPSase_L_chain_B.
InterProi IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami PF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PRINTSi PR00098. CPSASE.
SMARTi SM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsi TIGR01369. CPSaseII_lrg. 1 hit.
PROSITEi PS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The carB gene of Escherichia coli: a duplicated gene coding for the large subunit of carbamoyl-phosphate synthetase."
    Nyunoya H., Lusty C.J.
    Proc. Natl. Acad. Sci. U.S.A. 80:4629-4633(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-2.
    Strain: K12.
  2. "Multiple regulatory signals in the control region of the Escherichia coli carAB operon."
    Bouvier J., Patte J.-C., Stragier P.
    Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "DNA sequence of the carA gene and the control region of carAB: tandem promoters, respectively controlled by arginine and the pyrimidines, regulate the synthesis of carbamoyl-phosphate synthetase in Escherichia coli K-12."
    Piette J., Nyunoya H., Lusty C.J., Cunin R., Weyens G., Crabeel M., Charlier D.R.M., Glansdorff N., Pierard A.
    Proc. Natl. Acad. Sci. U.S.A. 81:4134-4138(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product."
    Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I.
    Biochemistry 36:6305-6316(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  9. "Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis."
    Thoden J.B., Miran S.G., Phillips J.C., Howard A.J., Raushel F.M., Holden H.M.
    Biochemistry 37:8825-8831(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  10. "The structure of carbamoyl phosphate synthetase determined to 2.1-A resolution."
    Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.
    Acta Crystallogr. D 55:8-24(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  11. "Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding."
    Thoden J.B., Wesenberg G., Raushel F.M., Holden H.M.
    Biochemistry 38:2347-2357(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  12. "The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway."
    Thoden J.B., Huang X., Raushel F.M., Holden H.M.
    Biochemistry 38:16158-16166(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  13. "The binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetase."
    Thoden J.B., Raushel F.M., Wesenberg G., Holden H.M.
    J. Biol. Chem. 274:22502-22507(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Entry informationi

Entry nameiCARB_ECOLI
AccessioniPrimary (citable) accession number: P00968
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi