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Protein

Carbamoyl-phosphate synthase large chain, C-terminal section

Gene

carB2

Organism
Aquifex aeolicus (strain VF5)
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi272 – 2721Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi284 – 2841Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi284 – 2841Magnesium or manganese 2PROSITE-ProRule annotation
Metal bindingi286 – 2861Magnesium or manganese 2PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi148 – 20558ATPPROSITE-ProRule annotationAdd
BLAST

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

BioCyciAAEO224324:GJBH-832-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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 537537Carbamoyl-phosphate synthase large chain, C-terminal sectionPRO_0000144985Add
BLAST

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 313192ATP-graspPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 397397Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni398 – 537140Allosteric domainAdd
BLAST

Domaini

Corresponds to the C-terminal section.

Sequence similaritiesi

Belongs to the CarB family.Curated
Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
InParanoidiO67233.
KOiK01955.
OMAiCVQAVFA.
OrthoDBiEOG6J1DC6.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.1380. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. CPSase_L_D2. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

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.
PATRICi20959582. VBIAquAeo85532_0911.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO67233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_1172.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC07203; AAC07203; aq_1172.
GeneIDi1192579.
KEGGiaae:aq_1172.
PATRICi20959582. VBIAquAeo85532_0911.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
InParanoidiO67233.
KOiK01955.
OMAiCVQAVFA.
OrthoDBiEOG6J1DC6.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.
BioCyciAAEO224324:GJBH-832-MONOMER.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.1380. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. CPSase_L_D2. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.

Entry informationi

Entry nameiCARB2_AQUAE
AccessioniPrimary (citable) accession number: O67233
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

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.