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Q55338 (PYRB_SULAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:Saci_1596
OrganismSulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP]
Taxonomic identifier330779 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. HAMAP-Rule MF_00001

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. HAMAP-Rule MF_00001

Subunit structure

Heterooligomer of catalytic and regulatory chains.

Sequence similarities

Belongs to the ATCase/OTCase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Aspartate carbamoyltransferase HAMAP-Rule MF_00001
PRO_0000113258

Secondary structure

......................................................... 299
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q55338 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6A283A584F94E32D

FASTA29934,171
        10         20         30         40         50         60 
MKHIISAYNF SRDELEDIFA LTDKYSKNLN DTRKILSGKT ISIAFFEPST RTYLSFQKAI 

        70         80         90        100        110        120 
INLGGDVIGF SGEESTSVAK GENLADTIRM LNNYSDGIVM RHKYDGASRF ASEISDIPVI 

       130        140        150        160        170        180 
NAGDGKHEHP TQAVIDIYTI NKHFNTIDGL VFALLGDLKY ARTVNSLLRI LTRFRPKLVY 

       190        200        210        220        230        240 
LISPQLLRAR KEILDELNYP VKEVENPFEV INEVDVLYVT RIQKERFVDE MEYEKIKGSY 

       250        260        270        280        290 
IVSLDLANKM KKDSIILHPL PRVNEIDRKV DKTTKAKYFE QASYGVPVRM SILTKIYGE 

« Hide

References

« Hide 'large scale' references
[1]"Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification and characterization."
Durbecq V., Thia-Toong T.-L., Charlier D.R.M., Villeret V., Roovers M., Wattiez R., Legrain C., Glansdorff N.
Eur. J. Biochem. 264:233-241(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
[2]"Genes of de novo pyrimidine biosynthesis from the hyperthermoacidophilic crenarchaeote Sulfolobus acidocaldarius: novel organization in a bipolar operon."
Thia-Toong T.-L., Roovers M., Durbecq V., Gigot D., Glansdorff N., Charlier D.R.M.
J. Bacteriol. 184:4430-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
[3]"The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota."
Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.
J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99872 Genomic DNA. Translation: CAA68165.1.
AJ459777 Genomic DNA. Translation: CAD31976.1.
CP000077 Genomic DNA. Translation: AAY80909.1.
RefSeqYP_256202.1. NC_007181.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PG5X-ray2.60A2-299[»]
2BE9X-ray2.60A2-299[»]
ProteinModelPortalQ55338.
SMRQ55338. Positions 1-299.
ModBaseSearch...

Protein-protein interaction databases

IntActQ55338. 1 interaction.
STRING330779.Saci_1596.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY80909; AAY80909; Saci_1596.
GeneID3474279.
KEGGsai:Saci_1596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0540.
HOGENOMHOG000022685.
KOK00609.
OMAYGVPVRM.
ProtClustDBPRK00856.

Enzyme and pathway databases

BioCycSACI330779:GH9J-1583-MONOMER.
BRENDA2.1.3.2. 6160.
UniPathwayUPA00070; UER00116.

Family and domain databases

HAMAPMF_00001. Asp_carb_tr.
InterProIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
[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...

Other

EvolutionaryTraceQ55338.

Entry information

Entry namePYRB_SULAC
AccessionPrimary (citable) accession number: Q55338
Secondary accession number(s): Q4J8H1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 93 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families