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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

Mn2+UniRule annotationNote: Binds 4 Mn2+ ions per subunit.UniRule annotation

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from bicarbonate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase catalytic chain (pyrB)
  3. Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi285 – 2851Manganese 1UniRule annotation
Metal bindingi299 – 2991Manganese 1UniRule annotation
Metal bindingi299 – 2991Manganese 25 Publications
Metal bindingi301 – 3011Manganese 25 Publications
Metal bindingi829 – 8291Manganese 31 Publication
Metal bindingi841 – 8411Manganese 31 Publication
Metal bindingi841 – 8411Manganese 42 Publications
Metal bindingi843 – 8431Manganese 42 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPUniRule annotationAdd
BLAST
Nucleotide bindingi705 – 76258ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

  • amino acid binding Source: EcoliWiki
  • ATP binding Source: EcoCyc
  • carbamoyl-phosphate synthase (ammonia) activity Source: EcoliWiki
  • carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  • metal ion binding Source: EcoliWiki
  • nucleotide binding Source: EcoliWiki

GO - Biological processi

  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • arginine biosynthetic process Source: GO_Central
  • cellular amino acid biosynthetic process Source: EcoliWiki
  • pyrimidine nucleobase biosynthetic process Source: EcoliWiki
  • urea cycle Source: GO_Central
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.
BRENDAi6.3.5.5. 2026.
SABIO-RKP00968.
UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase large chainUniRule annotation (EC:6.3.5.5UniRule annotation)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chainUniRule annotation
Gene namesi
Name:carB1 Publication
Synonyms:pyrA
Ordered Locus Names:b0033, JW0031
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10135. carB.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 10731072Carbamoyl-phosphate synthase large chainPRO_0000145004Add
BLAST

Proteomic databases

EPDiP00968.
PaxDbiP00968.
PRIDEiP00968.

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.UniRule annotation

Binary interactionsi

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

Protein-protein interaction databases

BioGridi4259726. 22 interactions.
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 1UniRule annotationAdd
BLAST
Domaini679 – 870192ATP-grasp 2UniRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
InParanoidiP00968.
KOiK01955.
OMAiSTAYMYS.
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. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
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]
PfamiPF02786. 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.
WP_001126348.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73144; AAC73144; b0033.
BAB96602; BAB96602; BAB96602.
GeneIDi944775.
KEGGiecj:JW0031.
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.
PIRiA01198. SYECCP.
RefSeqiNP_414574.1. NC_000913.3.
WP_001126348.1. NZ_LN832404.1.

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...

Protein-protein interaction databases

BioGridi4259726. 22 interactions.
DIPiDIP-1025N.
IntActiP00968. 13 interactions.
MINTiMINT-1255866.
STRINGi511145.b0033.

Proteomic databases

EPDiP00968.
PaxDbiP00968.
PRIDEiP00968.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73144; AAC73144; b0033.
BAB96602; BAB96602; BAB96602.
GeneIDi944775.
KEGGiecj:JW0031.
eco:b0033.
PATRICi32115159. VBIEscCol129921_0031.

Organism-specific databases

EchoBASEiEB0133.
EcoGeneiEG10135. carB.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
InParanoidiP00968.
KOiK01955.
OMAiSTAYMYS.
PhylomeDBiP00968.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.
BioCyciEcoCyc:CARBPSYN-LARGE.
ECOL316407:JW0031-MONOMER.
MetaCyc:CARBPSYN-LARGE.
BRENDAi6.3.5.5. 2026.
SABIO-RKP00968.

Miscellaneous databases

EvolutionaryTraceiP00968.
PROiP00968.

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. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
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]
PfamiPF02786. 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]
ProtoNetiSearch...

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: September 7, 2016
This is version 176 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.