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P41008 (PYRB_BACCL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 66. 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
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length308 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

Subunit structure

Homotrimer.

Sequence similarities

Belongs to the ATCase/OTCase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 308308Aspartate carbamoyltransferase HAMAP MF_00001
PRO_0000113091

Sequences

Sequence LengthMass (Da)Tools
P41008 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: FAAA34EA1620291A

FASTA30834,871
        10         20         30         40         50         60 
MTHLFALSEL PLDEIHRLLD EAERFRSGRI WRPAAPMYVA NLFFEPSTRT KCSFEMAERK 

        70         80         90        100        110        120 
LGLHVIPFDP ERSSVQKGET LYDTVRTLEA IGVDAVVIRH HEDAYFEALR HAVGIPIINA 

       130        140        150        160        170        180 
GDGCGHHPTQ SLLDLLTIRQ EFGAFTGLTV AIIGDIRHSR VARSNAEVLT RLGANVLFSG 

       190        200        210        220        230        240 
PEEWKDETNP YGTYVEVDEA IARADVVMLL RIQHERHAET MGLTKEEYHA RYGLTLERAR 

       250        260        270        280        290        300 
RMKSGAIILH PAPVNRGVEI ASELVEAKAS RIFKQMENGV YVRMAVLKRA MEGRMEHGRM 


AEKWHVVQ 

« Hide

References

[1]"Molecular characterization of pyrimidine biosynthesis genes from the thermophile Bacillus caldolyticus."
Ghim S.Y., Nielsen P., Neuhard J.
Microbiology 140:479-491(1994) [PubMed: 7516791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 405 / NBRC 15313 / YP-T.
[2]"The pyrimidine biosynthesis operon of the thermophile Bacillus caldolyticus includes genes for uracil phosphoribosyltransferase and uracil permease."
Ghim S.Y., Neuhard J.
J. Bacteriol. 176:3698-3707(1994) [PubMed: 8206848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
Strain: DSM 405 / NBRC 15313 / YP-T.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73308 Genomic DNA. Translation: CAA51736.1.
X76083 Genomic DNA. Translation: CAA53698.1.
PIRI40166.

3D structure databases

ProteinModelPortalP41008.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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]
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_BACCL
AccessionPrimary (citable) accession number: P41008
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: September 21, 2011
This is version 66 of the entry and version 2 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