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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: -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

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: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
SMRiO28994
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 328ATP-grasp 1UniRule annotationAdd BLAST196
Domaini680 – 871ATP-grasp 2UniRule annotationAdd BLAST192
Domaini938 – 1076MGS-likePROSITE-ProRule annotationAdd BLAST139

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG01594 Archaea
COG0458 LUCA
KOiK01955
OMAiAVFPFNK
OrthoDBiPOG093Z00Z2

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, 1 hit
PS51855 MGS, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCARB_ARCFU
AccessioniPrimary (citable) accession number: O28994
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 128 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