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Protein

Carbamoyl-phosphate synthase large chain, C-terminal section

Gene

carB2

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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, N-terminal section (carB1), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain, C-terminal section (carB2)
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, N-terminal section (carB1), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain, C-terminal section (carB2)
  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 bindingi358 – 3581Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi370 – 3701Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi370 – 3701Magnesium or manganese 2PROSITE-ProRule annotation
Metal bindingi372 – 3721Magnesium or manganese 2PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi234 – 29158ATPPROSITE-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

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:MJ1381
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 618618Carbamoyl-phosphate synthase large chain, C-terminal sectionPRO_0000145076Add
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

STRINGi243232.MJ_1381.

Structurei

3D structure databases

ProteinModelPortaliQ58776.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini208 – 399192ATP-graspPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 477397Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni478 – 618141Allosteric 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

eggNOGiarCOG01594. Archaea.
COG0458. LUCA.
InParanoidiQ58776.
KOiK01955.
OMAiCVQAVFA.
PhylomeDBiQ58776.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 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.
IPR005480. CarbamoylP_synth_lsu_oligo.
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.
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. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q58776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMEKLKEIL LKAKKLGFSD KQIANLLGMD EIEVRDLRKK LNIIPLYKMV
60 70 80 90 100
DTCAAEFEAK TPYYYSAYET FVYKEQDESN PSDRKKVIII GSGPIRIGQG
110 120 130 140 150
IEFDYSSVHA VLALKEMGIE AIIINNNPET VSTDYDTSDK LYFEPITFEE
160 170 180 190 200
VLNIAEREKE KGELLGVIVQ FGGQTAINLA MKLKNAGVNI LGTTPENINA
210 220 230 240 250
AEDREEFSKL LKKLNIPQAE GGTAYTKEEA LEIAKRIGYP VLVRPSYVLG
260 270 280 290 300
GRAMQIVYSE DELIEYMEEA VKVSEEHPVL IDKFLEDAIE LDVDAVCDGE
310 320 330 340 350
SVLIGAIMEH IEEAGVHSGD SATVIPPQTL PKEIIDTVID YTAKLARALN
360 370 380 390 400
IVGLLNVQYA VKDGVVYVLE ANPRASRTVP YVSKSVGIPL AKLATKIMLG
410 420 430 440 450
KKLEELIKDY DVEKVAEKVW IAKPKYVSIK EAVFPFQKLP GVDPVLGPEM
460 470 480 490 500
KSTGEAIGID KDFGRAYYKA QLSANMELPI VGNVFISVRD RDKKHIVDVA
510 520 530 540 550
KKLHELGFTI YATEGTAKVL RENGIPAILV KKISESPNDN ILKLMRDGKM
560 570 580 590 600
HLIINTSSGK KAKSDGYYIR RAAVDLGIPY ITTIPGAKAA VKAIEAVKTG
610
ELSVYSLDEL DARIKNRF
Length:618
Mass (Da):68,453
Last modified:November 1, 1996 - v1
Checksum:i8C3D4D9C192A954E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99391.1.
PIRiD64472.

Genome annotation databases

EnsemblBacteriaiAAB99391; AAB99391; MJ_1381.
KEGGimja:MJ_1381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99391.1.
PIRiD64472.

3D structure databases

ProteinModelPortaliQ58776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99391; AAB99391; MJ_1381.
KEGGimja:MJ_1381.

Phylogenomic databases

eggNOGiarCOG01594. Archaea.
COG0458. LUCA.
InParanoidiQ58776.
KOiK01955.
OMAiCVQAVFA.
PhylomeDBiQ58776.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 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.
IPR005480. CarbamoylP_synth_lsu_oligo.
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.
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. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARB2_METJA
AccessioniPrimary (citable) accession number: Q58776
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: November 1, 1996
Last modified: February 17, 2016
This is version 117 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 M.jannaschii (MJ1378 and MJ1381).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.