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Q81WE9 (PYRB_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate carbamoyltransferase

EC=2.1.3.2
Alternative name(s):
Aspartate transcarbamylase
Short name=ATCase
Gene names
Name:pyrB
Ordered Locus Names:BA_4028, GBAA_4028, BAS3740
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Sequence similarities

Belongs to the ATCase/OTCase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304Aspartate carbamoyltransferase HAMAP MF_00001
PRO_0000113089

Sequences

Sequence LengthMass (Da)Tools
Q81WE9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7E4FE09447EE773E

FASTA30434,722
        10         20         30         40         50         60 
MSHLLTMSEL SEVEISEILK DAEDFANGKE SKTTEQTFVA NLFFENSTRT RFSFEVAEKR 

        70         80         90        100        110        120 
LGLDVLNFSA DASSVQKGET LYDTIRTLES IGTKAVVIRH EQDRYFDELK DQVNIPILNA 

       130        140        150        160        170        180 
GDGCGNHPTQ CLLDLLTIKQ EFGRFEGLKI AIVGDVRHSR VARSNAEALT KLGATIYFAS 

       190        200        210        220        230        240 
PEEWKDEDNT FGTYKPLDEL VPEVDVMMLL RVQHERHDHY ETDIMKEYHE KHGLTVEREK 

       250        260        270        280        290        300 
RMKEGSIIMH PAPVNRDVEI ASELVECERS RIFKQMENGV YVRMAVLKRA LPNVLGGMKH 


ELFV 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP27755.1.
AE017334 Genomic DNA. Translation: AAT33145.1.
AE017225 Genomic DNA. Translation: AAT56042.1.
RefSeqNP_846269.1. NC_003997.3.
YP_020670.1. NC_007530.2.
YP_029991.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81WE9.
ModBaseSearch...

Protein-protein interaction databases

IntActQ81WE9. 5 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000010378; EBBACP00000010134; EBBACG00000010370.
EBBACT00000016180; EBBACP00000015801; EBBACG00000016172.
EBBACT00000024430; EBBACP00000023915; EBBACG00000024421.
GeneID1086640.
2819233.
2852925.
GenomeReviewsGene locus BA_4028 in contig AE016879_GR.
Gene locus BAS3740 in contig AE017225_GR.
Gene locus GBAA_4028 in contig AE017334_GR.
KEGGban:BA_4028.
bar:GBAA_4028.
bat:BAS3740.
TIGRBA_4028.
GBAA_4028.

Phylogenomic databases

GeneTreeEBGT00050000002562.
HOGENOMHBG579429.
OMALQRERMS.
ProtClustDBPRK00856.

Enzyme and pathway databases

BioCycBANT260799:BAS3740-MONOMER.
BANT261594:GBAA4028-MONOMER.

Family and domain databases

HAMAPMF_00001. Asp_carb_tr.
[Tree]
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR002082. Asp_carbamoyltransf_euk.
[Graphical view]
KOK00609.
PfamPF00185. OTCace. 1 hit.
PF02729. OTCace_N. 1 hit.
[Graphical view]
PRINTSPR00100. AOTCASE.
PR00101. ATCASE.
SUPFAMSSF53671. Asp/Orn_carbamoyltranf. 1 hit.
TIGRFAMsTIGR00670. Asp_carb_tr. 1 hit.
PROSITEPS00097. CARBAMOYLTRANSFERASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRB_BACAN
AccessionPrimary (citable) accession number: Q81WE9
Secondary accession number(s): Q6HUJ7, Q6KNT2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families