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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: Annotation score: 4 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 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

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: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

Complete GO annotation...

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini131 – 325ATP-grasp 1UniRule annotationAdd BLAST195
Domaini673 – 863ATP-grasp 2UniRule annotationAdd BLAST191

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
Contains 2 ATP-grasp domains.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG01594. Archaea.
COG0458. LUCA.
HOGENOMiHOG000234583.
InParanoidiQ59969.
KOiK01955.
OMAiSTAYMYS.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.20. 2 hits.
HAMAPiMF_01210_A. CPSase_L_chain_A. 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.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ59969.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0641.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK40949; AAK40949; SSO0641.
GeneIDi27426943.
KEGGisso:SSO0641.

Phylogenomic databases

eggNOGiarCOG01594. Archaea.
COG0458. LUCA.
HOGENOMiHOG000234583.
InParanoidiQ59969.
KOiK01955.
OMAiSTAYMYS.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.20. 2 hits.
HAMAPiMF_01210_A. CPSase_L_chain_A. 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.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARB_SULSO
AccessioniPrimary (citable) accession number: Q59969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 127 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.