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Protein

Carbamoyl-phosphate synthase large chain, C-terminal section

Gene

carB2

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Caution

CarB is split into two genes in A.aeolicus (AQ_1172 and AQ_2101).Curated

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese 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.
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain, C-terminal section (carB2), Carbamoyl-phosphate synthase large chain, N-terminal section (carB1), 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.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain, C-terminal section (carB2), Carbamoyl-phosphate synthase large chain, N-terminal section (carB1), 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 bindingi272Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi284Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi284Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi286Magnesium or manganese 2PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi148 – 205ATPPROSITE-ProRule 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

BioCyciAAEO224324:G1G15-826-MONOMER
UniPathwayiUPA00068; UER00171
UPA00070; UER00115

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase large chain, C-terminal section (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:carB2
Ordered Locus Names:aq_1172
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001449851 – 537Carbamoyl-phosphate synthase large chain, C-terminal sectionAdd BLAST537

Proteomic databases

PRIDEiO67233

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.By similarity

Protein-protein interaction databases

STRINGi224324.aq_1172

Structurei

3D structure databases

ProteinModelPortaliO67233
SMRiO67233
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini122 – 313ATP-graspPROSITE-ProRule annotationAdd BLAST192
Domaini396 – 537MGS-likePROSITE-ProRule annotationAdd BLAST142

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 397Carbamoyl phosphate synthetic domainAdd BLAST397
Regioni398 – 537Allosteric domainAdd BLAST140

Domaini

Corresponds to the C-terminal section.

Sequence similaritiesi

Belongs to the CarB family.Curated

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
HOGENOMiHOG000234582
InParanoidiO67233
KOiK01955
OMAiCVQAVFA
OrthoDBiPOG091H01IP

Family and domain databases

CDDicd01424 MGS_CPS_II, 1 hit
Gene3Di3.40.50.1380, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
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, 1 hit
PF02142 MGS, 1 hit
PRINTSiPR00098 CPSASE
SMARTiView protein in SMART
SM00851 MGS, 1 hit
SUPFAMiSSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

O67233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKVVILGS GPNRIGQGIE FDYACVHAVF SLQEEGYYAV MVNCNPETVS
60 70 80 90 100
TDYDTADKLY FEPIVFEHVM DIIEREKPEG VILQFGGQTP LKLALPLQKN
110 120 130 140 150
GVKILGTKPE SIDKAEDREL FRELIIELGL KQPPSGTART KEEALKIAKE
160 170 180 190 200
IGFPVLVRPS YVLGGRAMRI VYDEEELKEY LEEAVSVSHE RPVLIDKFLD
210 220 230 240 250
NSIELDVDAV SDGKDVLIGA VMEHIEEAGV HSGDSATSIP PYSLSKEIVE
260 270 280 290 300
EVKEQTRKLA VALEVKGLIN VQYAVQNNEV YVLEVNPRAS RTVPFVSKSI
310 320 330 340 350
GYPLAKIATK VAIGKSLREI LPEVFERLEK GEAHFASDFL PKEKKIFSVK
360 370 380 390 400
EVVFPWKRFP EVDPILGPEM KSTGEVMGID KEFGLAYYKA QLSAGYRLPE
410 420 430 440 450
KGNLFISVAD RDKPKILELA KEFEKLGFGI YATSGTYKFL KEHGVNAKRV
460 470 480 490 500
LKVSEGRPNV VDMIINGEIH LVINTPSGKR EKSDAYYIRR ACVQFNVPYY
510 520 530
TTMRAGYAVL EAIKSIKKLK EEGKGLSVHS LQEIYNI
Length:537
Mass (Da):60,037
Last modified:August 1, 1998 - v1
Checksum:i9C777FD2ED8085F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA Translation: AAC07203.1
PIRiF70400
RefSeqiNP_213797.1, NC_000918.1
WP_010880735.1, NC_000918.1

Genome annotation databases

EnsemblBacteriaiAAC07203; AAC07203; aq_1172
GeneIDi1192579
KEGGiaae:aq_1172
PATRICifig|224324.8.peg.911

Similar proteinsi

Entry informationi

Entry nameiCARB2_AQUAE
AccessioniPrimary (citable) accession number: O67233
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 1, 1998
Last modified: May 23, 2018
This is version 127 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
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Main funding by: National Institutes of Health