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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
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 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 (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 bindingi282Magnesium or manganese 1UniRule annotation1
Metal bindingi296Magnesium or manganese 1UniRule annotation1
Metal bindingi296Magnesium or manganese 2UniRule annotation1
Metal bindingi298Magnesium or manganese 2UniRule annotation1
Metal bindingi822Magnesium or manganese 3UniRule annotation1
Metal bindingi834Magnesium or manganese 3UniRule annotation1
Metal bindingi834Magnesium or manganese 4UniRule annotation1
Metal bindingi836Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi157 – 214ATPUniRule annotationAdd BLAST58
Nucleotide bindingi699 – 756ATPUniRule 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

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:SSO0641
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001450841 – 1051Carbamoyl-phosphate synthase large chainAdd BLAST1051

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.

Protein-protein interaction databases

STRINGi273057.SSO0641

Structurei

3D structure databases

ProteinModelPortaliQ59969
SMRiQ59969
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini131 – 325ATP-grasp 1UniRule annotationAdd BLAST195
Domaini673 – 863ATP-grasp 2UniRule annotationAdd BLAST191
Domaini930 – 1051MGS-likePROSITE-ProRule annotationAdd BLAST122

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 399Carboxyphosphate synthetic domainAdd BLAST399
Regioni400 – 548Oligomerization domainAdd BLAST149
Regioni549 – 930Carbamoyl phosphate synthetic domainAdd BLAST382
Regioni931 – 1051Allosteric domainAdd BLAST121

Sequence similaritiesi

Belongs to the CarB family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG01594 Archaea
COG0458 LUCA
HOGENOMiHOG000234583
InParanoidiQ59969
KOiK01955
OMAiAVFPFNK
OrthoDBiPOG093Z00Z2

Family and domain databases

Gene3Di1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
HAMAPiMF_01210_A CPSase_L_chain_A, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
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
PS00867 CPSASE_2, 1 hit
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

Q59969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRETPKKVLV IGSGPIKIAE AAEFDYSGSQ ALKALKEEGI ETVLVNSNVA
60 70 80 90 100
TVQTSKKFAD KLYMLPVVWW AVEKVIEKER PDGIMIGFGG QTALNVGVDL
110 120 130 140 150
HKKGVLQKYN VKVLGTQIDG IEKALSREKF RETMIENNLP VPPSLSARSE
160 170 180 190 200
EEAIKNAKIV GYPVMVRVSF NLGGRGSMVA WTEEDLKKNI RRALSQSYIG
210 220 230 240 250
EVLLEKYLYH WIELEYEVMR DKKGNSAVIA CIENLDPMGV HTGESTVVAP
260 270 280 290 300
CQTLDNLEYQ NMRTYTIEVA RSINLIGECN VQFALNPRGY EYYIIETNPR
310 320 330 340 350
MSRSSALASK ATGYPLAYVS AKLALGYELH EVINKVSGRT CACFEPSLDY
360 370 380 390 400
IVTKIPRWDL SKFENVDQSL ATEMMSVGEV MSIGRSFEES LQKAIRMLDI
410 420 430 440 450
GEPGVVGGKV YESNMSKEEA LKYLKERRPY WFLYAAKAFK EGATINEVYE
460 470 480 490 500
VTGINEFFLN KIKGLVDFYE TLRKLKEIDK ETLKLAKKLG FSDEQISKAL
510 520 530 540 550
NKSTEYVRKI RYETNTIPVV KLIDTLAGEW PAVTNYMYLT YNGTEDDIEF
560 570 580 590 600
SQGNKLLIIG AGGFRIGVSV EFDWSVVSLM EAGSKYFDEV AVLNYNPETV
610 620 630 640 650
STDWDIARKL YFDEISVERV LDLIKKEKFR YVATFSGGQI GNSIAKELEE
660 670 680 690 700
NGVRLLGTSG SSVDIAENRE KFSKLLDKLG ISQPDWISAT SLGEIKKFAN
710 720 730 740 750
EVGFPVLVRP SYVLSGSSMK IAYSEEELYE YVRRATEISP KYPVVISKYI
760 770 780 790 800
ENAIEAEIDG VSDGNKVLGI TLEHIEEAGV HSGDATMSIP FRKLSENNVN
810 820 830 840 850
RMRENVLNIA RELNIKGPFN VQFVVKENTP YIIELNLRAS RSMPFSSKAK
860 870 880 890 900
GINLINESMK AIFDGLDFSE DYYEPPSKYW AVKSAQFSWS QLRGAYPFLG
910 920 930 940 950
PEMKSTGEAA SFGVTFYDAL LKSWLSSMPN RIPNKNGIAL VYGNKNLDYL
960 970 980 990 1000
KDTADNLTRF GLTVYSISEL PLQDIETIDK MKAEELVRAK KVEIIVTDGY
1010 1020 1030 1040 1050
LKKFDYNIRR TAVDYNIPII LNGRLGYEVS KAFLNYDSLT FFEISEYGGG

I
Length:1,051
Mass (Da):118,204
Last modified:November 1, 1996 - v1
Checksum:i07FE2415283B799D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33768 Genomic DNA Translation: AAA99059.1
Y18930 Genomic DNA Translation: CAB57658.1
AE006641 Genomic DNA Translation: AAK40949.1
PIRiT43253
RefSeqiWP_009991180.1, NC_002754.1

Genome annotation databases

EnsemblBacteriaiAAK40949; AAK40949; SSO0641
GeneIDi27426943
KEGGisso:SSO0641
PATRICifig|273057.12.peg.646

Similar proteinsi

Entry informationi

Entry nameiCARB_SULSO
AccessioniPrimary (citable) accession number: Q59969
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 137 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