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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
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 (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 (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 bindingi285Magnesium or manganese 1UniRule annotation1
Metal bindingi299Magnesium or manganese 1UniRule annotation1
Metal bindingi299Magnesium or manganese 2UniRule annotation1
Metal bindingi301Magnesium or manganese 2UniRule annotation1
Metal bindingi825Magnesium or manganese 3UniRule annotation1
Metal bindingi837Magnesium or manganese 3UniRule annotation1
Metal bindingi837Magnesium or manganese 4UniRule annotation1
Metal bindingi839Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi700 – 758ATPUniRule annotationAdd BLAST59

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

BioCyciTTHE262724:G1G0N-253-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:TT_C0247
OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Taxonomic identifieri262724 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000592 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001450591 – 1028Carbamoyl-phosphate synthase large chainAdd BLAST1028

Proteomic databases

PRIDEiP96495

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

STRINGi262724.TTC0247

Structurei

3D structure databases

ProteinModelPortaliP96495
SMRiP96495
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 328ATP-grasp 1UniRule annotationAdd BLAST196
Domaini674 – 866ATP-grasp 2UniRule annotationAdd BLAST193
Domaini934 – 1028MGS-likePROSITE-ProRule annotationAdd BLAST95

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 409Carboxyphosphate synthetic domainAdd BLAST409
Regioni410 – 549Oligomerization domainAdd BLAST140
Regioni550 – 933Carbamoyl phosphate synthetic domainAdd BLAST384
Regioni934 – 1028Allosteric domainAdd BLAST95

Sequence similaritiesi

Belongs to the CarB family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
KOiK01955
OMAiAVFPFNK

Family and domain databases

Gene3Di1.10.1030.10, 1 hit
HAMAPiMF_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
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF02786 CPSase_L_D2, 2 hits
PF02787 CPSase_L_D3, 1 hit
PRINTSiPR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SUPFAMiSSF48108 SSF48108, 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.

P96495-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPRRDLKKI LIIGSGPITI GQAAEFDYSG TQAVKALRGA GYRVVLVNSN
60 70 80 90 100
PATIMTDPEL AERTYIEPLD LEHLEGILAR EAPDALLPTL GGQTGLNLAM
110 120 130 140 150
ALYEEGILQK YGVELIGAKA EAIRKGEDRE AFQEAMRRID LEVPRGQLVG
160 170 180 190 200
SVEEGLHFAR EVGFPVVVRP SFTLGGTGGG IAHDEAELVE VLSRGLTLSP
210 220 230 240 250
VHTALVEESV LGWKEFELEV MRDHADTVVI ITSIENVDPM GVHTGDSITV
260 270 280 290 300
APAQTLSDVE YQRMRDAAKA IIREIGVETG GSNIQFAVDP KTGRQVVIEM
310 320 330 340 350
NPRVSRSSAL ASKATGFPIA KIAALLAVGY RLDELPNDIT RKTPASFEPT
360 370 380 390 400
IDYVVVKIPR FAFEKFRPLR NTLGELKDEL TTQMKSVGEV MAIGRTFKEA
410 420 430 440 450
LMKALRGLER DVRALAGVRT EELEKKLYPN PDRVYAVMEL LRRGMPVEEL
460 470 480 490 500
YQATRIDPWF LHQMKEIVEA EEWLKTHPPK DREDWRFYKG LGLTDRRIGE
510 520 530 540 550
LLGKGEKEVR AERKALGVVP VYKTVDTCAA EFEAYTPYHY STYELEDEVW
560 570 580 590 600
PSQKPKVVIL GSGPIRIGQG VEFDYATVHA VWALKEAGFE TIMVNSNPET
610 620 630 640 650
VSTDYDTADR LYFEPLTLED VLNIVEHEKP IGVIATLGGQ TPLKLAKGLE
660 670 680 690 700
EAGVRLLGTP FSAIHQAEDR EAFHALCQRL GIPQPEGRVA QSPEEALRLA
710 720 730 740 750
PEVGFPLLVR PSYVLGGRAM QVVRDEGELK RYLEEVYAPL EERPSILLDR
760 770 780 790 800
FLEGAIELDV DALSDGQEVM VAGIMEHVER AGVHSGDSAT LLPPVHVPEE
810 820 830 840 850
ALKKVRDYTR RLALTLGVRG LLNVQYAVVG EEVYVLEANP RASRTVPFVS
860 870 880 890 900
KAIGVPLAKL AALIAVGKTL KELGVRDLDP VPPYYAAKEV VIPWIKFPGV
910 920 930 940 950
IPELGPEMRS TGESMGIDQD PYLAYYKAEL GAGQRLPLSG QVRFIGEGLE
960 970 980 990 1000
DLKALYQEAG FALTEGQDYD LLISLVPDPE LRRAVERGLP FITTREGAWW
1010 1020
SLKAILRARE SGLRVQSLQD WHQKAPRG
Length:1,028
Mass (Da):113,609
Last modified:May 24, 2004 - v2
Checksum:iDD032A40E389B4CE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti329G → P in CAA72256 (Ref. 1) Curated1
Sequence conflicti489K → Q in CAA72256 (Ref. 1) Curated1
Sequence conflicti536T → P in CAA72256 (Ref. 1) Curated1
Sequence conflicti576A → P in CAA72256 (Ref. 1) Curated1
Sequence conflicti613F → V in CAA72256 (Ref. 1) Curated1
Sequence conflicti628E → Q in CAA72256 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11467 Genomic DNA Translation: CAA72256.1
AE017221 Genomic DNA Translation: AAS80595.1
RefSeqiWP_011172699.1, NC_005835.1

Genome annotation databases

EnsemblBacteriaiAAS80595; AAS80595; TT_C0247
KEGGitth:TT_C0247

Similar proteinsi

Entry informationi

Entry nameiCARB_THET2
AccessioniPrimary (citable) accession number: P96495
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: May 24, 2004
Last modified: March 28, 2018
This is version 120 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

Complete proteome

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