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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 4 Mg2+ or Mn2+ ions per subunit.By similarity

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 (pyraA)
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 (pyraA)
  2. Aspartate carbamoyltransferase (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 bindingi284Magnesium or manganese 1UniRule annotation1
Metal bindingi298Magnesium or manganese 1UniRule annotation1
Metal bindingi298Magnesium or manganese 2UniRule annotation1
Metal bindingi300Magnesium or manganese 2UniRule annotation1
Metal bindingi820Magnesium or manganese 3UniRule annotation1
Metal bindingi832Magnesium or manganese 3UniRule annotation1
Metal bindingi832Magnesium or manganese 4UniRule annotation1
Metal bindingi834Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi697 – 754ATPUniRule annotationAdd BLAST58

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

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:carBUniRule annotation
Ordered Locus Names:EF_1716
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000663501 – 1060Carbamoyl-phosphate synthase large chainAdd BLAST1060

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.UniRule annotation

Protein-protein interaction databases

STRINGi226185.EF1716.

Structurei

3D structure databases

ProteinModelPortaliQ834E2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 327ATP-grasp 1UniRule annotationAdd BLAST195
Domaini671 – 861ATP-grasp 2UniRule annotationAdd BLAST191

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 401Carboxyphosphate synthetic domainAdd BLAST401
Regioni402 – 546Oligomerization domainAdd BLAST145
Regioni547 – 929Carbamoyl phosphate synthetic domainAdd BLAST383
Regioni930 – 1060Allosteric domainAdd BLAST131

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.
KOiK01955.
OMAiSTAYMYS.

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.

Q834E2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRTDIKKI MVIGSGPIII GQAAEFDYAG TQACLALKEE GYEVVLVNSN
60 70 80 90 100
PATIMTDKEI ADHVYIEPIT LEFVSRILRK ERPDALLPTL GGQTGLNMAM
110 120 130 140 150
ELSESGILDE LNVELLGTKL SAIDQAEDRD LFKQLMEELE QPIPESEIVN
160 170 180 190 200
TVEQAVAFAK RIGYPIIVRP AFTLGGTGGG MCDTEEELRQ IAENGLKLSP
210 220 230 240 250
VTQCLIEKSI AGFKEIEYEV MRDSADNAIV VCNMENFDPV GIHTGDSIVF
260 270 280 290 300
APSQTLSDYE YQMLRDASLK IIRALKIEGG CNVQLALDPH SFNYYVIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMKNPVTG TTYAEFEPAL
360 370 380 390 400
DYVVSKIPRW PFDKFEKGAR ELGTQMKATG EVMAIGRNIE ESLLKAVRSL
410 420 430 440 450
EIGAYHNELA ELSHVSDLEL TKKMVHAQDD RLFYLSEAIR RGYSIEELQS
460 470 480 490 500
LTKIDLFFLD KLLHIIEIET ALESHVDNVA VLKEAKQNGF SDRKIAALWG
510 520 530 540 550
QTEQAIADFR RANQIVPVYK MVDTCAAEFE SHTPYFYSTY EVENESNVSK
560 570 580 590 600
KPSVLVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
610 620 630 640 650
DFSVSDKLYF EPLTLEDVMN VIDLENPIGV IVQFGGQTAI NLAEPLTKQG
660 670 680 690 700
VKILGTTIED LDRAENRDLF EQALQELAIP QPPGDTATSA EEAVVIADRI
710 720 730 740 750
GYPVLVRPSY VLGGRAMEIV ENQKDLEDYM RHAVKASPEH PVLVDSYLLG
760 770 780 790 800
QECEVDAICD GETVLIPGIM EHIERAGVHS GDSMAVYPPQ YLSQEIQATI
810 820 830 840 850
ADYTKKLALG LNCVGMMNIQ FVIHENRVYV IEVNPRASRT VPFLSKITGI
860 870 880 890 900
PMAQVATKAI LGEKLTDLGY QDGLYPESKQ VHVKAPVFSF TKLQKVDTYL
910 920 930 940 950
GPEMKSTGEV MGSDYYLEKA LYKAFEASGL HLPSYGAVLF TIADETKEEA
960 970 980 990 1000
LEIAKRFSAI GYSLVATEGT ADFLAKHQLP VKKVTKISNP EGETVLDVIR
1010 1020 1030 1040 1050
NGNAQVVIST MDKNRSSANQ DGFSIRREAV EHGIPLFTSL DTANAILKVL
1060
ESRAFTTEAI
Length:1,060
Mass (Da):116,717
Last modified:June 1, 2003 - v1
Checksum:iD45594C43C42C245
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO81492.1.
RefSeqiNP_815422.1. NC_004668.1.
WP_010774214.1. NZ_KE136528.1.

Genome annotation databases

EnsemblBacteriaiAAO81492; AAO81492; EF_1716.
GeneIDi1200608.
KEGGiefa:EF1716.
PATRICi21853776. VBIEntFae7065_1614.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO81492.1.
RefSeqiNP_815422.1. NC_004668.1.
WP_010774214.1. NZ_KE136528.1.

3D structure databases

ProteinModelPortaliQ834E2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226185.EF1716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO81492; AAO81492; EF_1716.
GeneIDi1200608.
KEGGiefa:EF1716.
PATRICi21853776. VBIEntFae7065_1614.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
KOiK01955.
OMAiSTAYMYS.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

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_ENTFA
AccessioniPrimary (citable) accession number: Q834E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: November 30, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.