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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: -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 (glutamine-hydrolyzing) (pyrAB2), 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)DescriptionActionsGraphical viewLength
Metal bindingi284Magnesium or manganese 1By similarity1
Metal bindingi298Magnesium or manganese 1By similarity1
Metal bindingi298Magnesium or manganese 2By similarity1
Metal bindingi300Magnesium or manganese 2By similarity1
Metal bindingi820Magnesium or manganese 3By similarity1
Metal bindingi832Magnesium or manganese 3By similarity1
Metal bindingi832Magnesium or manganese 4By similarity1
Metal bindingi834Magnesium or manganese 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPBy similarityAdd BLAST58
Nucleotide bindingi697 – 754ATPBy similarityAdd BLAST58

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processPyrimidine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciLPLA220668:G1GW0-2312-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)DescriptionActionsGraphical viewLength
ChainiPRO_00001450141 – 1058Carbamoyl-phosphate synthase pyrimidine-specific large chainAdd BLAST1058

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
SMRiP77886
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 327ATP-grasp 1Add BLAST195
Domaini671 – 861ATP-grasp 2Add BLAST191
Domaini930 – 1058MGS-likePROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 401Carboxyphosphate synthetic domainAdd BLAST401
Regioni402 – 546Oligomerization domainAdd BLAST145
Regioni547 – 929Carbamoyl phosphate synthetic domainAdd BLAST383
Regioni930 – 1058Allosteric domainAdd BLAST129

Sequence similaritiesi

Belongs to the CarB family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
HOGENOMiHOG000234582
KOiK01955
OMAiAVFPFNK

Family and domain databases

CDDicd01424 MGS_CPS_II, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.40.50.1380, 1 hit
HAMAPiMF_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, 2 hits
PS51855 MGS, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti160K → E in CAA91005 (PubMed:8982065).Curated1
Sequence conflicti410 – 411PA → ST in CAA91005 (PubMed:8982065).Curated2
Sequence conflicti444P → Q in CAA91005 (PubMed:8982065).Curated1
Sequence conflicti862D → G in CAA91005 (PubMed:8982065).Curated1
Sequence conflicti992R → H in CAA91005 (PubMed:8982065).Curated1
Sequence conflicti1003I → V in CAA91005 (PubMed:8982065).Curated1

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
PATRICifig|220668.9.peg.2260

Similar proteinsi

Entry informationi

Entry nameiCARB_LACPL
AccessioniPrimary (citable) accession number: P77886
Secondary accession number(s): F9URI2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 25, 2003
Last modified: March 28, 2018
This is version 123 of the entry and version 2 of the sequence. See 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

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