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P00968

- CARB_ECOLI

UniProt

P00968 - CARB_ECOLI

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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

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.

Cofactori

Mn2+Note: Binds 4 Mn(2+) 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 4By similarity
Metal bindingi843 – 8431Manganese 4By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPBy similarityAdd
BLAST
Nucleotide bindingi705 – 76258ATPBy similarityAdd
BLAST

GO - Molecular functioni

  1. amino acid binding Source: EcoliWiki
  2. ATP binding Source: EcoCyc
  3. carbamoyl-phosphate synthase (ammonia) activity Source: EcoliWiki
  4. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  5. metal ion binding Source: EcoliWiki
  6. nucleotide binding Source: EcoliWiki

GO - Biological processi

  1. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  2. arginine biosynthetic process Source: UniProtKB-UniPathway
  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 chainPRO_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

1
1073
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135Combined sources
Helixi25 – 4016Combined sources
Beta strandi43 – 475Combined sources
Helixi54 – 563Combined sources
Helixi58 – 603Combined sources
Beta strandi61 – 655Combined sources
Helixi71 – 8111Combined sources
Beta strandi84 – 874Combined sources
Beta strandi89 – 913Combined sources
Helixi92 – 10413Combined sources
Helixi107 – 1115Combined sources
Helixi120 – 1278Combined sources
Helixi129 – 13810Combined sources
Beta strandi145 – 1517Combined sources
Helixi152 – 16211Combined sources
Beta strandi164 – 1707Combined sources
Turni175 – 1784Combined sources
Beta strandi180 – 1845Combined sources
Helixi185 – 19814Combined sources
Beta strandi204 – 2085Combined sources
Beta strandi213 – 22210Combined sources
Beta strandi228 – 23811Combined sources
Helixi244 – 2463Combined sources
Beta strandi249 – 2524Combined sources
Helixi258 – 27518Combined sources
Beta strandi279 – 28810Combined sources
Turni290 – 2923Combined sources
Beta strandi295 – 3039Combined sources
Helixi306 – 31510Combined sources
Helixi319 – 3279Combined sources
Helixi332 – 3343Combined sources
Turni338 – 3425Combined sources
Beta strandi344 – 3463Combined sources
Beta strandi353 – 3619Combined sources
Helixi364 – 3663Combined sources
Beta strandi382 – 3909Combined sources
Helixi391 – 40111Combined sources
Beta strandi402 – 4054Combined sources
Beta strandi407 – 4093Combined sources
Helixi420 – 42910Combined sources
Helixi435 – 44410Combined sources
Helixi449 – 4568Combined sources
Helixi460 – 47920Combined sources
Helixi481 – 4833Combined sources
Helixi486 – 4949Combined sources
Helixi499 – 5057Combined sources
Helixi510 – 51910Combined sources
Beta strandi525 – 5284Combined sources
Beta strandi541 – 5477Combined sources
Beta strandi557 – 5593Combined sources
Beta strandi561 – 5655Combined sources
Helixi576 – 59116Combined sources
Beta strandi595 – 5995Combined sources
Helixi606 – 6083Combined sources
Beta strandi612 – 6176Combined sources
Helixi623 – 63311Combined sources
Beta strandi636 – 6394Combined sources
Beta strandi641 – 6433Combined sources
Helixi645 – 6484Combined sources
Helixi651 – 6566Combined sources
Beta strandi661 – 6644Combined sources
Helixi666 – 6738Combined sources
Helixi675 – 68511Combined sources
Beta strandi692 – 6943Combined sources
Helixi698 – 70811Combined sources
Beta strandi710 – 7156Combined sources
Turni721 – 7244Combined sources
Beta strandi725 – 7284Combined sources
Helixi731 – 74010Combined sources
Beta strandi751 – 7544Combined sources
Beta strandi760 – 7689Combined sources
Beta strandi773 – 78311Combined sources
Helixi789 – 7913Combined sources
Beta strandi794 – 7974Combined sources
Beta strandi799 – 8013Combined sources
Helixi803 – 81917Combined sources
Beta strandi824 – 8329Combined sources
Beta strandi837 – 8437Combined sources
Helixi850 – 8578Combined sources
Helixi861 – 8699Combined sources
Helixi874 – 8774Combined sources
Beta strandi886 – 8949Combined sources
Helixi896 – 8994Combined sources
Beta strandi915 – 9239Combined sources
Helixi924 – 93411Combined sources
Beta strandi941 – 9488Combined sources
Helixi951 – 9544Combined sources
Helixi957 – 96610Combined sources
Beta strandi970 – 9734Combined sources
Helixi975 – 9828Combined sources
Turni983 – 9853Combined sources
Beta strandi989 – 9924Combined sources
Turni994 – 9963Combined sources
Beta strandi998 – 10003Combined sources
Helixi1001 – 10077Combined sources
Beta strandi1011 – 10155Combined sources
Helixi1020 – 10256Combined sources
Helixi1027 – 10359Combined sources
Beta strandi1039 – 10435Combined sources
Helixi1044 – 105411Combined sources
Turni1058 – 10603Combined sources
Helixi1065 – 10706Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00968.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0458.
HOGENOMiHOG000234582.
InParanoidiP00968.
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

        10         20         30         40         50
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN
60 70 80 90 100
PATIMTDPEM ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL
110 120 130 140 150
ELERQGVLEE FGVTMIGATA DAIDKAEDRR RFDVAMKKIG LETARSGIAH
160 170 180 190 200
TMEEALAVAA DVGFPCIIRP SFTMGGSGGG IAYNREEFEE ICARGLDLSP
210 220 230 240 250
TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM GIHTGDSITV
260 270 280 290 300
APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
310 320 330 340 350
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP
360 370 380 390 400
SIDYVVTKIP RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR
410 420 430 440 450
GLEVGATGFD PKVSLDDPEA LTKIRRELKD AGADRIWYIA DAFRAGLSVD
460 470 480 490 500
GVFNLTNIDR WFLVQIEELV RLEEKVAEVG ITGLNADFLR QLKRKGFADA
510 520 530 540 550
RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT AYMYSTYEEE
560 570 580 590 600
CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
610 620 630 640 650
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL
660 670 680 690 700
ARALEAAGVP VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM
710 720 730 740 750
AVEKAKEIGY PLVVRPSYVL GGRAMEIVYD EADLRRYFQT AVSVSNDAPV
760 770 780 790 800
LLDHFLDDAV EVDVDAICDG EMVLIGGIME HIEQAGVHSG DSACSLPAYT
810 820 830 840 850
LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI EVNPRAARTV
860 870 880 890 900
PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF
910 920 930 940 950
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR
960 970 980 990 1000
EGDKERVVDL AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH
1010 1020 1030 1040 1050
IQDRIKNGEY TYIINTTSGR RAIEDSRVIR RSALQYKVHY DTTLNGGFAT
1060 1070
AMALNADATE KVISVQEMHA QIK
Length:1,073
Mass (Da):117,842
Last modified:January 23, 2007 - v2
Checksum:iA09D019CBDFF8D2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P00968.
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: November 26, 2014
This is version 163 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