P05654 (PYRB_BACSU) Reviewed, UniProtKB/Swiss-Prot

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

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
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; (S)-dihydroorotate from bicarbonate: step 2/3. HAMAP MF_00001
Subunit structure	Homotrimer.
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 Reference proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Inferred from electronic annotation. Source: EC
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

Secondary structure

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304

Helix Strand Turn

Details...

Helix

7 – 9

3

Helix

12 – 26

15

Beta strand

38 – 45

8

Helix

49 – 60

12

Beta strand

64 – 68

5

Helix

81 – 90

10

Beta strand

95 – 99

5

Helix

106 – 112

7

Beta strand

117 – 119

3

Helix

128 – 142

15

Beta strand

149 – 153

5

Helix

160 – 171

12

Beta strand

175 – 178

4

Helix

182 – 184

3

Helix

197 – 203

7

Beta strand

205 – 209

5

Turn

214 – 216

3

Turn

227 – 229

3

Helix

234 – 237

4

Beta strand

245 – 247

3

Helix

260 – 262

3

Helix

270 – 275

6

Helix

279 – 289

11

Sequences

	Sequence		Length	Mass (Da)
	P05654 [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 155:1758-1775(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. 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: 1906175] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

OWBSAC. A25015.

RefSeq

NP_389432.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AT2	X-ray	3.00	A/B/C	1-300	[»]
3R7D	X-ray	2.20	A/B/C	1-304	[»]
3R7F	X-ray	2.10	A/B/C	1-304	[»]
3R7L	X-ray	2.58	A/B/C/D/E/F	1-304	[»]

ProteinModelPortal

P05654.

SMR

P05654. Positions 1-289.

ModBase

Search...

PTM databases

PhosSite

P05654.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000002975; EBBACP00000002975; EBBACG00000002969.

GeneID

937734.

GenomeReviews

Gene locus BSU15490 in contig AL009126_GR.

KEGG

bsu:BSU15490.

NMPDR

fig|224308.1.peg.1551.

PATRIC

18974905. VBIBacSub10457_1644.

Organism-specific databases

GenoList

BSU15490. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000002562.

HOGENOM

HBG579429.

PhylomeDB

P05654.

ProtClustDB

PRK00856.

Enzyme and pathway databases

BioCyc

BSUB:BSU15490-MONOMER.

Family and domain databases

HAMAP

MF_00001. Asp_carb_tr.
[Tree]

InterPro

IPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002082. Asp_carbamoyltransf_euk.
[Graphical view]

KO

K00609.

Pfam

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

PRINTS

PR00100. AOTCASE.
PR00101. ATCASE.

SUPFAM

SSF53671. Asp/Orn_carbamoyltranf. 1 hit.

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:	January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program