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Protein

Carbamoyl-phosphate synthase pyrimidine-specific large chain

Gene

pyrAB

Organism
Bacillus subtilis (strain 168)
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

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 large chain (pyrAB), Carbamoyl-phosphate synthase pyrimidine-specific small chain (pyrAA)
  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

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

BioCyciBSUB:BSU15520-MONOMER.
SABIO-RKP25994.
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:BSU15520
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001449911 – 1071Carbamoyl-phosphate synthase pyrimidine-specific large chainAdd BLAST1071

Proteomic databases

PaxDbiP25994.
PRIDEiP25994.

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

IntActiP25994. 1 interactor.
STRINGi224308.Bsubs1_010100008576.

Structurei

3D structure databases

ProteinModelPortaliP25994.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 327ATP-grasp 1Add BLAST195
Domaini671 – 861ATP-grasp 2Add BLAST191

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 401Carboxyphosphate synthetic domainAdd BLAST401
Regioni402 – 546Oligomerization domainAdd BLAST145
Regioni547 – 929Carbamoyl phosphate synthetic domainAdd BLAST383
Regioni930 – 1071Allosteric domainAdd BLAST142

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234583.
InParanoidiP25994.
KOiK01955.
OMAiSTAYMYS.
PhylomeDBiP25994.

Family and domain databases

CDDicd01424. MGS_CPS_II. 1 hit.
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_A. CPSase_L_chain_A. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
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.
IPR033937. MGS_CPS_CarB.
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.

P25994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRVDINKI LVIGSGPIII GQAAEFDYAG TQACLALKEE GYEVILVNSN
60 70 80 90 100
PATIMTDTEM ADRVYIEPLT PEFLTRIIRK ERPDAILPTL GGQTGLNLAV
110 120 130 140 150
ELSERGVLAE CGVEVLGTKL SAIQQAEDRD LFRTLMNELN EPVPESEIIH
160 170 180 190 200
SLEEAEKFVS QIGFPVIVRP AYTLGGTGGG ICSNETELKE IVENGLKLSP
210 220 230 240 250
VHQCLLEKSI AGYKEIEYEV MRDSQDHAIV VCNMENIDPV GIHTGDSIVV
260 270 280 290 300
APSQTLSDRE YQLLRNVSLK LIRALGIEGG CNVQLALDPD SFQYYIIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK LAAKIAVGLS LDEMMNPVTG KTYAAFEPAL
360 370 380 390 400
DYVVSKIPRW PFDKFESANR KLGTQMKATG EVMAIGRTLE ESLLKAVRSL
410 420 430 440 450
EADVYHLELK DAADISDELL EKRIKKAGDE RLFYLAEAYR RGYTVEDLHE
460 470 480 490 500
FSAIDVFFLH KLFGIVQFEK ELKANAGDTD VLRRAKELGF SDQYISREWK
510 520 530 540 550
MKESELYSLR KQAGIAPVFK MVDTCAAEFE SETPYFYSTY EEENESVVTD
560 570 580 590 600
KKSVMVLGSG PIRIGQGVEF DYATVHSVWA IKQAGYEAII VNNNPETVST
610 620 630 640 650
DFSISDKLYF EPLTIEDVMH IIDLEQPMGV VVQFGGQTAI NLADELSARG
660 670 680 690 700
VKILGTSLED LDRAEDRDKF EQALGELGVP QPLGKTATSV NQAVSIASDI
710 720 730 740 750
GYPVLVRPSY VLGGRAMEIV YHEEELLHYM KNAVKINPQH PVLIDRYLTG
760 770 780 790 800
KEIEVDAVSD GETVVIPGIM EHIERAGVHS GDSIAVYPPQ SLTEDIKKKI
810 820 830 840 850
EQYTIALAKG LNIVGLLNIQ FVLSQGEVYV LEVNPRSSRT VPFLSKITGI
860 870 880 890 900
PMANLATKII LGQKLAAFGY TEGLQPEQQG VFVKAPVFSF AKLRRVDITL
910 920 930 940 950
GPEMKSTGEV MGKDSTLEKA LYKALIASGI QIPNYGSVLL TVADKDKEEG
960 970 980 990 1000
LAIAKRFHAI GYNILATEGT AGYLKEASIP AKVVGKIGQD GPNLLDVIRN
1010 1020 1030 1040 1050
GEAQFVINTL TKGKQPARDG FRIRRESVEN GVACLTSLDT AEAILRVLES
1060 1070
MTFRADQMPA VNTNQEAAVT I
Length:1,071
Mass (Da):117,650
Last modified:May 1, 1992 - v1
Checksum:i195E33CFC5C6222C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59757 Genomic DNA. Translation: AAA21270.1.
AL009126 Genomic DNA. Translation: CAB13426.1.
PIRiF39845.
RefSeqiNP_389435.1. NC_000964.3.
WP_003232113.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13426; CAB13426; BSU15520.
GeneIDi936608.
KEGGibsu:BSU15520.
PATRICi18974911. VBIBacSub10457_1647.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59757 Genomic DNA. Translation: AAA21270.1.
AL009126 Genomic DNA. Translation: CAB13426.1.
PIRiF39845.
RefSeqiNP_389435.1. NC_000964.3.
WP_003232113.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP25994.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP25994. 1 interactor.
STRINGi224308.Bsubs1_010100008576.

Proteomic databases

PaxDbiP25994.
PRIDEiP25994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13426; CAB13426; BSU15520.
GeneIDi936608.
KEGGibsu:BSU15520.
PATRICi18974911. VBIBacSub10457_1647.

Phylogenomic databases

eggNOGiENOG4105CU6. Bacteria.
COG0458. LUCA.
HOGENOMiHOG000234583.
InParanoidiP25994.
KOiK01955.
OMAiSTAYMYS.
PhylomeDBiP25994.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.
BioCyciBSUB:BSU15520-MONOMER.
SABIO-RKP25994.

Family and domain databases

CDDicd01424. MGS_CPS_II. 1 hit.
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_A. CPSase_L_chain_A. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
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.
IPR033937. MGS_CPS_CarB.
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...

Entry informationi

Entry nameiCARB_BACSU
AccessioniPrimary (citable) accession number: P25994
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 30, 2016
This is version 130 of the entry and version 1 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.