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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)DescriptionActionsGraphical viewLength
Metal bindingi285Manganese 1UniRule annotation1
Metal bindingi299Manganese 1UniRule annotation1
Metal bindingi299Manganese 25 Publications1
Metal bindingi301Manganese 25 Publications1
Metal bindingi829Manganese 31 Publication1
Metal bindingi841Manganese 31 Publication1
Metal bindingi841Manganese 42 Publications1
Metal bindingi843Manganese 42 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi705 – 762ATPUniRule annotationAdd BLAST58

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001450042 – 1073Carbamoyl-phosphate synthase large chainAdd BLAST1072

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

Structurei

Secondary structure

11073
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 13Combined sources5
Helixi25 – 40Combined sources16
Beta strandi43 – 47Combined sources5
Helixi54 – 56Combined sources3
Helixi58 – 60Combined sources3
Beta strandi61 – 65Combined sources5
Helixi71 – 81Combined sources11
Beta strandi84 – 87Combined sources4
Beta strandi89 – 91Combined sources3
Helixi92 – 104Combined sources13
Helixi107 – 111Combined sources5
Helixi120 – 127Combined sources8
Helixi129 – 138Combined sources10
Beta strandi145 – 151Combined sources7
Helixi152 – 162Combined sources11
Beta strandi164 – 170Combined sources7
Turni175 – 178Combined sources4
Beta strandi180 – 184Combined sources5
Helixi185 – 198Combined sources14
Beta strandi204 – 208Combined sources5
Beta strandi213 – 222Combined sources10
Beta strandi228 – 238Combined sources11
Helixi244 – 246Combined sources3
Beta strandi249 – 252Combined sources4
Helixi258 – 275Combined sources18
Beta strandi279 – 288Combined sources10
Turni290 – 292Combined sources3
Beta strandi295 – 303Combined sources9
Helixi306 – 315Combined sources10
Helixi319 – 327Combined sources9
Helixi332 – 334Combined sources3
Turni338 – 342Combined sources5
Beta strandi344 – 346Combined sources3
Beta strandi353 – 361Combined sources9
Helixi364 – 366Combined sources3
Beta strandi382 – 390Combined sources9
Helixi391 – 401Combined sources11
Beta strandi402 – 405Combined sources4
Beta strandi407 – 409Combined sources3
Helixi420 – 429Combined sources10
Helixi435 – 444Combined sources10
Helixi449 – 456Combined sources8
Helixi460 – 479Combined sources20
Helixi481 – 483Combined sources3
Helixi486 – 494Combined sources9
Helixi499 – 505Combined sources7
Helixi510 – 519Combined sources10
Beta strandi525 – 528Combined sources4
Beta strandi541 – 547Combined sources7
Beta strandi557 – 559Combined sources3
Beta strandi561 – 565Combined sources5
Helixi576 – 591Combined sources16
Beta strandi595 – 599Combined sources5
Helixi606 – 608Combined sources3
Beta strandi612 – 617Combined sources6
Helixi623 – 633Combined sources11
Beta strandi636 – 639Combined sources4
Beta strandi641 – 643Combined sources3
Helixi645 – 648Combined sources4
Helixi651 – 656Combined sources6
Beta strandi661 – 664Combined sources4
Helixi666 – 673Combined sources8
Helixi675 – 685Combined sources11
Beta strandi692 – 694Combined sources3
Helixi698 – 708Combined sources11
Beta strandi710 – 715Combined sources6
Turni721 – 724Combined sources4
Beta strandi725 – 728Combined sources4
Helixi731 – 740Combined sources10
Beta strandi751 – 754Combined sources4
Beta strandi760 – 768Combined sources9
Beta strandi773 – 783Combined sources11
Helixi789 – 791Combined sources3
Beta strandi794 – 797Combined sources4
Beta strandi799 – 801Combined sources3
Helixi803 – 819Combined sources17
Beta strandi824 – 832Combined sources9
Beta strandi837 – 843Combined sources7
Helixi850 – 857Combined sources8
Helixi861 – 869Combined sources9
Helixi874 – 877Combined sources4
Beta strandi886 – 894Combined sources9
Helixi896 – 899Combined sources4
Beta strandi915 – 923Combined sources9
Helixi924 – 934Combined sources11
Beta strandi941 – 948Combined sources8
Helixi951 – 954Combined sources4
Helixi957 – 966Combined sources10
Beta strandi970 – 973Combined sources4
Helixi975 – 982Combined sources8
Turni983 – 985Combined sources3
Beta strandi989 – 992Combined sources4
Turni994 – 996Combined sources3
Beta strandi998 – 1000Combined sources3
Helixi1001 – 1007Combined sources7
Beta strandi1011 – 1015Combined sources5
Helixi1020 – 1025Combined sources6
Helixi1027 – 1035Combined sources9
Beta strandi1039 – 1043Combined sources5
Helixi1044 – 1054Combined sources11
Turni1058 – 1060Combined sources3
Helixi1065 – 1070Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00968.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 328ATP-grasp 1UniRule annotationAdd BLAST196
Domaini679 – 870ATP-grasp 2UniRule annotationAdd BLAST192

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 403Carboxyphosphate synthetic domainUniRule annotationAdd BLAST402
Regioni404 – 553Oligomerization domainUniRule annotationAdd BLAST150
Regioni554 – 936Carbamoyl phosphate synthetic domainUniRule annotationAdd BLAST383
Regioni937 – 1073Allosteric domainUniRule annotationAdd BLAST137

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

CDDicd01424. MGS_CPS_II. 1 hit.
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.
IPR033937. MGS_CPS_CarB.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259726. 22 interactors.
DIPiDIP-1025N.
IntActiP00968. 13 interactors.
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

CDDicd01424. MGS_CPS_II. 1 hit.
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.
IPR033937. MGS_CPS_CarB.
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: November 30, 2016
This is version 179 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.