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Protein

Aspartate carbamoyltransferase

Gene

pyrB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 2 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU15490-MONOMER.
BRENDAi2.1.3.2. 658.
SABIO-RKP05654.
UniPathwayiUPA00070; UER00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate carbamoyltransferase (EC:2.1.3.2)
Alternative name(s):
Aspartate transcarbamylase
Short name:
ATCase
Gene namesi
Name:pyrB
Ordered Locus Names:BSU15490
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Aspartate carbamoyltransferasePRO_0000113099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei303 – 3031Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05654.

PTM databases

iPTMnetiP05654.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008561.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Helixi12 – 2615Combined sources
Turni33 – 364Combined sources
Beta strandi38 – 458Combined sources
Helixi49 – 6012Combined sources
Beta strandi64 – 696Combined sources
Helixi73 – 764Combined sources
Beta strandi77 – 793Combined sources
Helixi81 – 9111Combined sources
Beta strandi95 – 995Combined sources
Turni103 – 1053Combined sources
Helixi106 – 1127Combined sources
Beta strandi117 – 1204Combined sources
Helixi128 – 14215Combined sources
Beta strandi149 – 1546Combined sources
Helixi156 – 1583Combined sources
Helixi160 – 17112Combined sources
Beta strandi175 – 1806Combined sources
Helixi182 – 1843Combined sources
Beta strandi192 – 1943Combined sources
Helixi197 – 2037Combined sources
Beta strandi205 – 2095Combined sources
Turni214 – 2163Combined sources
Helixi220 – 2245Combined sources
Helixi226 – 2305Combined sources
Helixi234 – 2374Combined sources
Beta strandi245 – 2473Combined sources
Turni254 – 2563Combined sources
Helixi260 – 2623Combined sources
Helixi270 – 28920Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AT2X-ray3.00A/B/C1-300[»]
3R7DX-ray2.20A/B/C1-304[»]
3R7FX-ray2.10A/B/C1-304[»]
3R7LX-ray2.58A/B/C/D/E/F1-304[»]
ProteinModelPortaliP05654.
SMRiP05654. Positions 1-289.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05654.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATCase/OTCase family.Curated

Phylogenomic databases

eggNOGiENOG4105CXT. Bacteria.
COG0540. LUCA.
HOGENOMiHOG000022685.
InParanoidiP05654.
KOiK00609.
OMAiWCDVANM.
OrthoDBiEOG61KBJZ.
PhylomeDBiP05654.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05654-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHLTTMSEL STEEIKDLLQ TAQELKSGKT DNQLTGKFAA NLFFEPSTRT
60 70 80 90 100
RFSFEVAEKK LGMNVLNLDG TSTSVQKGET LYDTIRTLES IGVDVCVIRH
110 120 130 140 150
SEDEYYEELV SQVNIPILNA GDGCGQHPTQ SLLDLMTIYE EFNTFKGLTV
160 170 180 190 200
SIHGDIKHSR VARSNAEVLT RLGARVLFSG PSEWQDEENT FGTYVSMDEA
210 220 230 240 250
VESSDVVMLL RIQNERHQSA VSQEGYLNKY GLTVERAERM KRHAIIMHPA
260 270 280 290 300
PVNRGVEIDD SLVESEKSRI FKQMKNGVFI RMAVIQRALQ TNVKRGEAAY

VISH
Length:304
Mass (Da):34,224
Last modified:June 16, 2009 - v2
Checksum:i3742CA07346E15FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871R → C in AAA22685 (PubMed:3015959).Curated
Sequence conflicti287 – 2871R → C in AAA21267 (PubMed:1709162).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13128 Genomic DNA. Translation: AAA22685.1.
M59757 Genomic DNA. Translation: AAA21267.1.
AL009126 Genomic DNA. Translation: CAB13423.2.
PIRiA25015. OWBSAC.
RefSeqiNP_389432.2. NC_000964.3.
WP_003245123.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13423; CAB13423; BSU15490.
GeneIDi937734.
KEGGibsu:BSU15490.
PATRICi18974905. VBIBacSub10457_1644.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13128 Genomic DNA. Translation: AAA22685.1.
M59757 Genomic DNA. Translation: AAA21267.1.
AL009126 Genomic DNA. Translation: CAB13423.2.
PIRiA25015. OWBSAC.
RefSeqiNP_389432.2. NC_000964.3.
WP_003245123.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AT2X-ray3.00A/B/C1-300[»]
3R7DX-ray2.20A/B/C1-304[»]
3R7FX-ray2.10A/B/C1-304[»]
3R7LX-ray2.58A/B/C/D/E/F1-304[»]
ProteinModelPortaliP05654.
SMRiP05654. Positions 1-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008561.

PTM databases

iPTMnetiP05654.

Proteomic databases

PaxDbiP05654.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13423; CAB13423; BSU15490.
GeneIDi937734.
KEGGibsu:BSU15490.
PATRICi18974905. VBIBacSub10457_1644.

Phylogenomic databases

eggNOGiENOG4105CXT. Bacteria.
COG0540. LUCA.
HOGENOMiHOG000022685.
InParanoidiP05654.
KOiK00609.
OMAiWCDVANM.
OrthoDBiEOG61KBJZ.
PhylomeDBiP05654.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00116.
BioCyciBSUB:BSU15490-MONOMER.
BRENDAi2.1.3.2. 658.
SABIO-RKP05654.

Miscellaneous databases

EvolutionaryTraceiP05654.

Family and domain databases

Gene3Di3.40.50.1370. 2 hits.
HAMAPiMF_00001. Asp_carb_tr.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[Graphical view]
PfamiPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMiSSF53671. SSF53671. 1 hit.
TIGRFAMsiTIGR00670. asp_carb_tr. 1 hit.
PROSITEiPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB)."
    Lerner C.G., Switzer R.L.
    J. Biol. Chem. 261:11156-11165(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon."
    Quinn C.L., Stephenson B.T., Switzer R.L.
    J. Biol. Chem. 266:9113-9127(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 287.
  5. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.
  6. "Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0-A resolution."
    Stevens R.C., Reinisch K.M., Lipscomb W.N.
    Proc. Natl. Acad. Sci. U.S.A. 88:6087-6091(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiPYRB_BACSU
AccessioniPrimary (citable) accession number: P05654
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: June 16, 2009
Last modified: February 17, 2016
This is version 141 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.