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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: -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

Keywordsi

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

Enzyme and pathway databases

BioCyciEFAE226185:G1G0C-1694-MONOMER
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
SMRiQ834E2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 327ATP-grasp 1UniRule annotationAdd BLAST195
Domaini671 – 861ATP-grasp 2UniRule annotationAdd BLAST191
Domaini930 – 1060MGS-likePROSITE-ProRule annotationAdd BLAST131

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
KOiK01955
OMAiAVFPFNK

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.

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
PATRICifig|226185.45.peg.1796

Similar proteinsi

Entry informationi

Entry nameiCARB_ENTFA
AccessioniPrimary (citable) accession number: Q834E2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2003
Last modified: March 28, 2018
This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health