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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
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 (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 bindingi830Magnesium or manganese 3UniRule annotation1
Metal bindingi842Magnesium or manganese 3UniRule annotation1
Metal bindingi842Magnesium or manganese 4UniRule annotation1
Metal bindingi844Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi706 – 763ATPUniRule 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:AF_1274
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
Proteomesi
  • UP000002199 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001450711 – 1076Carbamoyl-phosphate synthase large chainAdd BLAST1076

Proteomic databases

PRIDEiO28994.

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

STRINGi224325.AF1274.

Structurei

3D structure databases

ProteinModelPortaliO28994.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 328ATP-grasp 1UniRule annotationAdd BLAST196
Domaini680 – 871ATP-grasp 2UniRule annotationAdd BLAST192

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 402Carboxyphosphate synthetic domainAdd BLAST402
Regioni403 – 555Oligomerization domainAdd BLAST153
Regioni556 – 939Carbamoyl phosphate synthetic domainAdd BLAST384
Regioni940 – 1076Allosteric domainAdd BLAST137

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.
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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O28994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKREDIRKI MVIGSGPIVI GQAAEFDYSG SQACKALREE GYEVVLVNSN
60 70 80 90 100
PATIMTDPEM ADRVYIEPLD AEIVAKIIER ETPDALLPTL GGQTALNLAV
110 120 130 140 150
QLTEMGVLDK YGVELIGAKF EAIKKAEDRE LFKEAMRKIG LDVPKSDVAH
160 170 180 190 200
DVSEALAIAD EIGYPVVVRP AFTLGGTGGG IAYNREELRE IAERGIKMSM
210 220 230 240 250
INQVLIEEGV LGWKEFELEV MRDLADNVVI ICSIENFDPM GVHTGDSITV
260 270 280 290 300
APAQTLTDVE YQYLRDAAIK IIREIGVETG GSNIQFAVHP ENGRVVAIEM
310 320 330 340 350
NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDEIPNDIT KETPASFEPT
360 370 380 390 400
IDYVVVKIPR FAFDKFPTAN QVLGSQMKSV GEVMAVGRTF EEALQKAIRS
410 420 430 440 450
LEIGRYGLGC DGKDKEVTME EIRERLRYPN ASRVFYIRYA LQKGMSVNEI
460 470 480 490 500
YELTKIDPWF IDKIKNLVEF EEQLKQIAER MSIEEVPKEI LKKAKELGYS
510 520 530 540 550
DRQLAVIFNT TEREVRRVRK GKGLRVVYKM VDTCAAEFEA KTPYYYSTYE
560 570 580 590 600
DENEALRSER KKVMILGAGP NRIGQGIEFD YCCVHAVFSL KDEGYETIMV
610 620 630 640 650
NCNPETVSTD YDTSDRLYFE PITHEDVMNI YENEQPEGVI VQFGGQTPLN
660 670 680 690 700
IARELEDSGA RILGTSVDSI DIAEDRERFA ELLERLNIPQ PENGIAHSLE
710 720 730 740 750
EAKEIARKIG FPVLVRPSYV LGGRAMEIVY DEETLERYIT EALEVSPEKP
760 770 780 790 800
ILIDKFLEDA IEVEVDALCD GEEVVIGGIM EHIEEAGVHS GDSACVLPPV
810 820 830 840 850
SLDEVTINTI VDYTRKLALA LNVVGLINIQ YAVKDGKVYV LEANPRASRT
860 870 880 890 900
VPFVSKATGI PLAKIAAKLM MGKKLRELGV KEKLKLKHVA VKEAVFPFIK
910 920 930 940 950
LPGVDPVLGP EMKSTGEVMG IDYDFGLAYY KAELAAGMKL PLKGTVFISV
960 970 980 990 1000
RRKDKNDRLL YLARKFKELG FRIIATDGTR DFLVQNGIEA DLILKISQGR
1010 1020 1030 1040 1050
PNILDAIVNG QVDLIINTPS GKRGRTEGYM IRRAAVDYGV AHITTLAGAM
1060 1070
AAVRAIEAVK SRKMVVKSIQ EYHEES
Length:1,076
Mass (Da):119,471
Last modified:January 1, 1998 - v1
Checksum:i3FC275F648E5949D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89970.1.
PIRiA69409.
RefSeqiWP_010878769.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB89970; AAB89970; AF_1274.
GeneIDi24794885.
KEGGiafu:AF_1274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000782 Genomic DNA. Translation: AAB89970.1.
PIRiA69409.
RefSeqiWP_010878769.1. NC_000917.1.

3D structure databases

ProteinModelPortaliO28994.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224325.AF1274.

Proteomic databases

PRIDEiO28994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB89970; AAB89970; AF_1274.
GeneIDi24794885.
KEGGiafu:AF_1274.

Phylogenomic databases

eggNOGiarCOG01594. Archaea.
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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARB_ARCFU
AccessioniPrimary (citable) accession number: O28994
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 119 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.