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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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 small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
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 small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
  2. Aspartate carbamoyltransferase catalytic subunit (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: GO_Central
  • metal ion binding Source: EcoliWiki
  • nucleotide binding Source: EcoliWiki

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CARBPSYN-LARGE
MetaCyc:CARBPSYN-LARGE
BRENDAi6.3.5.5 2026
SABIO-RKiP00968
UniPathwayi
UPA00068;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

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
carAP0A6F114EBI-546118,EBI-546107

Protein-protein interaction databases

BioGridi4259726, 41 interactors
ComplexPortaliCPX-1937 Carbamoyl phosphate synthetase complex
DIPiDIP-1025N
IntActiP00968, 14 interactors
STRINGi316385.ECDH10B_0034

Structurei

Secondary structure

11073
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
Domaini937 – 1073MGS-likePROSITE-ProRule annotationAdd BLAST137

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
HOGENOMiHOG000234582
InParanoidiP00968
KOiK01955
PhylomeDBiP00968

Family and domain databases

CDDicd01424 MGS_CPS_II, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.40.50.1380, 1 hit
HAMAPiMF_01210_A CPSase_L_chain_A, 1 hit
MF_01210_B CPSase_L_chain_B, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR033937 MGS_CPS_CarB
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF02786 CPSase_L_D2, 2 hits
PF02787 CPSase_L_D3, 1 hit
PF02142 MGS, 1 hit
PRINTSiPR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF48108 SSF48108, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits
TIGRFAMsiTIGR01369 CPSaseII_lrg, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00866 CPSASE_1, 2 hits
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 1 hit

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
PATRICifig|1411691.4.peg.2251

Similar proteinsi

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, 41 interactors
ComplexPortaliCPX-1937 Carbamoyl phosphate synthetase complex
DIPiDIP-1025N
IntActiP00968, 14 interactors
STRINGi316385.ECDH10B_0034

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
PATRICifig|1411691.4.peg.2251

Organism-specific databases

EchoBASEiEB0133
EcoGeneiEG10135 carB

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
HOGENOMiHOG000234582
InParanoidiP00968
KOiK01955
PhylomeDBiP00968

Enzyme and pathway databases

UniPathwayi
UPA00068;UER00171

UPA00070;UER00115

BioCyciEcoCyc:CARBPSYN-LARGE
MetaCyc:CARBPSYN-LARGE
BRENDAi6.3.5.5 2026
SABIO-RKiP00968

Miscellaneous databases

EvolutionaryTraceiP00968
PROiPR:P00968

Family and domain databases

CDDicd01424 MGS_CPS_II, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.40.50.1380, 1 hit
HAMAPiMF_01210_A CPSase_L_chain_A, 1 hit
MF_01210_B CPSase_L_chain_B, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR033937 MGS_CPS_CarB
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF02786 CPSase_L_D2, 2 hits
PF02787 CPSase_L_D3, 1 hit
PF02142 MGS, 1 hit
PRINTSiPR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF48108 SSF48108, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits
TIGRFAMsiTIGR01369 CPSaseII_lrg, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00866 CPSASE_1, 2 hits
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCARB_ECOLI
AccessioniPrimary (citable) accession number: P00968
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 194 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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