Reviewed, UniProtKB/Swiss-Prot P05654 (PYRB_BACSU)

Names and origin

Protein names

Recommended name:
    Aspartate carbamoyltransferase
    EC=2.1.3.2
Alternative name(s):
    Aspartate transcarbamylase
      Short name=ATCase

Gene names

Name:	pyrB
Ordered Locus Names:	BSU15490

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. HAMAP MF_00001
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6. HAMAP MF_00001
Subunit structure	Homotrimer. HAMAP MF_00001
Sequence similarities	Belongs to the ATCase/OTCase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro amino acid metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 304	304	Aspartate carbamoyltransferase HAMAP MF_00001		PRO_0000113099
Amino acid modifications
	Modified residue	303	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	287	1	R → C in AAA22685. Ref.1
	Sequence conflict	287	1	R → C in AAA21267. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P05654-1 [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 3742CA07346E15FE	FASTA	304	34,224
	10 20 30 40 50 60 MKHLTTMSEL STEEIKDLLQ TAQELKSGKT DNQLTGKFAA NLFFEPSTRT RFSFEVAEKK 70 80 90 100 110 120 LGMNVLNLDG TSTSVQKGET LYDTIRTLES IGVDVCVIRH SEDEYYEELV SQVNIPILNA 130 140 150 160 170 180 GDGCGQHPTQ SLLDLMTIYE EFNTFKGLTV SIHGDIKHSR VARSNAEVLT RLGARVLFSG 190 200 210 220 230 240 PSEWQDEENT FGTYVSMDEA VESSDVVMLL RIQNERHQSA VSQEGYLNKY GLTVERAERM 250 260 270 280 290 300 KRHAIIMHPA PVNRGVEIDD SLVESEKSRI FKQMKNGVFI RMAVIQRALQ TNVKRGEAAY VISH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3015959] [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: 1709162] [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: 9384377] [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 0:0-0(2009) [PubMed: 19383706] [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: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, MASS SPECTROMETRY.
[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: 1906175] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

M13128 Genomic DNA. Translation: AAA22685.1.
M59757 Genomic DNA. Translation: AAA21267.1.
AL009126 Genomic DNA. Translation: CAB13423.2.

PIR

OWBSAC. A25015.

RefSeq

NP_389432.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AT2	X-ray	3.00	A/B/C	1-300	[»]

ModBase

Search...

PTM databases

PhosSite

P05654.

Genome annotation databases

GeneID

937734.

GenomeReviews

Gene locus BSU15490 in contig AL009126_GR.

KEGG

bsu:BSU15490.

NMPDR

fig|224308.1.peg.1551.

Organism-specific databases

SubtiList

BG10713. pyrB. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P05654.

OMA

P05654. RTVVNLF.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU1551-MON.

BRENDA

2.1.3.2. 150.

Family and domain databases

HAMAP

MF_00001.
[Tree]

InterPro

IPR006132. Asp/Orn_carbamoyltranf_P_bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn_bd.
IPR002082. Aspartate_carbamoyltransf_euk.
[Graphical view]

Pfam

PF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]

PRINTS

PR00100. AOTCASE.
PR00101. ATCASE.

TIGRFAMs

TIGR00670. asp_carb_tr. 1 hit.

PROSITE

PS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PYRB_BACSU

Accession

Primary (citable) accession number: P05654

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	June 16, 2009
Last modified:	June 16, 2009
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)