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Protein

Carbamoyl-phosphate synthase pyrimidine-specific large chain

Gene

pyrAB

Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
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 4 Mg2+ or Mn2+ ions per subunit.By similarity

Enzyme regulationi

Inhibited by pyrimidines.

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 pyrimidine-specific small chain (pyrAA), Carbamoyl-phosphate synthase pyrimidine-specific large chain (pyrAB), Carbamoyl-phosphate synthase small chain (pyrAA2)
  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 bindingi284 – 2841Magnesium or manganese 1By similarity
Metal bindingi298 – 2981Magnesium or manganese 1By similarity
Metal bindingi298 – 2981Magnesium or manganese 2By similarity
Metal bindingi300 – 3001Magnesium or manganese 2By similarity
Metal bindingi820 – 8201Magnesium or manganese 3By similarity
Metal bindingi832 – 8321Magnesium or manganese 3By similarity
Metal bindingi832 – 8321Magnesium or manganese 4By similarity
Metal bindingi834 – 8341Magnesium or manganese 4By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPBy similarityAdd
BLAST
Nucleotide bindingi697 – 75458ATPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciLPLA220668-WGS:GSPK-2312-MONOMER.
UniPathwayiUPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase pyrimidine-specific large chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:pyrAB
Ordered Locus Names:lp_2700
OrganismiLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifieri220668 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000000432 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10581058Carbamoyl-phosphate synthase pyrimidine-specific large chainPRO_0000145014Add
BLAST

Proteomic databases

PRIDEiP77886.

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.

Protein-protein interaction databases

STRINGi220668.lp_2700.

Structurei

3D structure databases

ProteinModelPortaliP77886.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 327195ATP-grasp 1Add
BLAST
Domaini671 – 861191ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 401401Carboxyphosphate synthetic domainAdd
BLAST
Regioni402 – 546145Oligomerization domainAdd
BLAST
Regioni547 – 929383Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni930 – 1058129Allosteric domainAdd
BLAST

Sequence similaritiesi

Belongs to the CarB family.Curated
Contains 2 ATP-grasp domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
KOiK01955.
OMAiAVFPFNK.

Family and domain databases

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_B. CPSase_L_chain_B.
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.
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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77886-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRTDIHKI MVIGSGPIII GQAAEFDYSG TQACLALKEL DYEVVLVNSN
60 70 80 90 100
PATIMTDKEI ADQVYLEPIT LEFVSQILRK EHPDAILPTL GGQQGLNMAM
110 120 130 140 150
ELSKSGILDE LHIELLGTKL SAIDQAEDRE QFKALMEELG EPVPASGIAR
160 170 180 190 200
TVDEALAFAK QAGYPVIVRP AFTMGGTGGG IAETPQQLHD ITENGLALSP
210 220 230 240 250
VTQVLIEQSI AGYKEIEFEV MRDAADNAMV VCNMENFDPV GIHTGDSIVY
260 270 280 290 300
APVQTLADRE VQLLRDAALK IIRALKIEGG CNVQLALDPN SFNYYIIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK MAAKIAVGLH LDEIKNPVTG TTYAEFEPAL
360 370 380 390 400
DYVVCKIPRW PFDKFTHADR RLGTQMKATG EVMAIGRNIE EATLKAVRSL
410 420 430 440 450
EIGVHHVEEP ALRSVDDDVL SDKLIHAQDD RLFYLTEAIR RGYPIDELAE
460 470 480 490 500
LTKINVFFLD KLLHIIEIEQ ALRTHTDDIE TLTVAKRNGF ADQTVADYWH
510 520 530 540 550
ETIDQVRDFR LAHKLAPVYK MVDTCAGEFA SETPYYYGTY EFENESIVTK
560 570 580 590 600
RPSVLVLGSG PIRIGQGVEF DYATVHSVKA IQKAGYEAII MNSNPETVST
610 620 630 640 650
DFSVSDKLYF EPLTIEDVLN VIELEKPVGV IVQFGGQTAI NLAKPLADHG
660 670 680 690 700
IKILGTSVAD VNRAEDRDEF DKVIKALAIP QPAGDTASDE ATALAIADKL
710 720 730 740 750
GYPVLVRPSY VLGGRAMEIV KKRTDLDYYM HNAVKVSHDH PVLVDSYLVG
760 770 780 790 800
KECEVDAICD GQTVLIPGIM EHIERAGVHS GDSMAVYPPQ SLSAAVQAQI
810 820 830 840 850
VDYTEKLAIA LNCVGMMNIQ FVIHDDQVYV IEVNPRASRT VPFLSKVTNI
860 870 880 890 900
PMAQVATRAI LDQSLAEQGY QTGLVTPGPL VHVKAPVFSF SKLNRVDSLL
910 920 930 940 950
GPEMKSTGEV MGSDVTMAKA LYKAFEAAKL HVPSHGNVLL TVRDEDKPET
960 970 980 990 1000
VALAKRFHAL GYQLLATRGT ATALTTHGLP VTTVDKIDSG ERDLLHRMEA
1010 1020 1030 1040 1050
GEIQVVINTV SDEEQAENDG TLIRNTSIMH GIPLFTALDT VAAILQVRES

QSFVTQAL
Length:1,058
Mass (Da):115,757
Last modified:March 25, 2003 - v2
Checksum:i3A5DEDF82EB60C55
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601K → E in CAA91005 (PubMed:8982065).Curated
Sequence conflicti410 – 4112PA → ST in CAA91005 (PubMed:8982065).Curated
Sequence conflicti444 – 4441P → Q in CAA91005 (PubMed:8982065).Curated
Sequence conflicti862 – 8621D → G in CAA91005 (PubMed:8982065).Curated
Sequence conflicti992 – 9921R → H in CAA91005 (PubMed:8982065).Curated
Sequence conflicti1003 – 10031I → V in CAA91005 (PubMed:8982065).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54240 Genomic DNA. Translation: CAA91005.1.
AL935263 Genomic DNA. Translation: CCC79821.1.
RefSeqiWP_011101886.1. NC_004567.2.
YP_004890335.1. NC_004567.2.

Genome annotation databases

EnsemblBacteriaiCCC79821; CCC79821; lp_2700.
GeneIDi1062982.
KEGGilpl:lp_2700.
PATRICi22251305. VBILacPla27411_2260.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z54240 Genomic DNA. Translation: CAA91005.1.
AL935263 Genomic DNA. Translation: CCC79821.1.
RefSeqiWP_011101886.1. NC_004567.2.
YP_004890335.1. NC_004567.2.

3D structure databases

ProteinModelPortaliP77886.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi220668.lp_2700.

Proteomic databases

PRIDEiP77886.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCC79821; CCC79821; lp_2700.
GeneIDi1062982.
KEGGilpl:lp_2700.
PATRICi22251305. VBILacPla27411_2260.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234582.
KOiK01955.
OMAiAVFPFNK.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.
BioCyciLPLA220668-WGS:GSPK-2312-MONOMER.

Family and domain databases

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_B. CPSase_L_chain_B.
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.
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. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and organisation of the pyrimidine biosynthesis pathway genes in Lactobacillus plantarum: a PCR strategy for sequencing without cloning."
    Elagoez A., Abdi A., Hubert J.-C., Kammerer B.
    Gene 182:37-43(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.
  3. "In Lactobacillus plantarum, carbamoyl phosphate is synthesized by two carbamoyl-phosphate synthetases (CPS): carbon dioxide differentiates the arginine-repressed from the pyrimidine-regulated CPS."
    Nicoloff H., Hubert J.-C., Bringel F.
    J. Bacteriol. 182:3416-3422(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: ATCC 8014 / CCM 1904 / DSM 20205 / NCDO 82 / NCIB 6376.

Entry informationi

Entry nameiCARB_LACPL
AccessioniPrimary (citable) accession number: P77886
Secondary accession number(s): F9URI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 25, 2003
Last modified: November 11, 2015
This is version 111 of the entry and version 2 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.