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Q59653 (PYRB_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PA0402
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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

Heterododecamer of 6 active PyrB subunits and 6 non-catalytic PyrC' subunits By similarity.

Sequence similarities

Belongs to the ATCase/OTCase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Aspartate carbamoyltransferase HAMAP-Rule MF_00001
PRO_0000113176

Experimental info

Sequence conflict2061R → A in AAA25976. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59653 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: 2DC90450FA2E42E9

FASTA33436,629
        10         20         30         40         50         60 
MPTDAKRPLQ LNDQGQLRHF ISLDGLPREL LTEILDTADS FLEVGARAVK KVPLLRGKTV 

        70         80         90        100        110        120 
CNVFFENSTR TRTTFELAAQ RLSADVISLN VSTSSTSKGE TLTDTLRNLE AMAADMFVVR 

       130        140        150        160        170        180 
HSDSGAAHFI AEHVSPNVAV INGGDGRHAH PTQGMLDMLT IRRHKGNFEQ LSVAIVGDIL 

       190        200        210        220        230        240 
HSRVARSNML ALKTLGCPDI RVIAPRTLLP IGLEEQYGVR VFTNADEGLK DVDVVIMLRL 

       250        260        270        280        290        300 
QRERMQGGLL PSEGEFFKLY GLTEKRLKLA KPDAIVMHPG PINRGVEIES AVADGAQSVI 

       310        320        330 
LNQVTYGIAI RMAVLSMAMS GQNTQRQLEQ EDAE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19649 Genomic DNA. Translation: AAA25976.1.
AE004091 Genomic DNA. Translation: AAG03791.1.
PIRH83595.
RefSeqNP_249093.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ59653.
SMRQ59653. Positions 17-314.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA0402.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID878267.
KEGGpae:PA0402.
PATRIC19835044. VBIPseAer58763_0423.

Organism-specific databases

PseudoCAPPA0402.

Phylogenomic databases

eggNOGCOG0540.
KOK00609.
OMALTIRQHK.
ProtClustDBPRK00856.

Enzyme and pathway databases

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...

Entry information

Entry namePYRB_PSEAE
AccessionPrimary (citable) accession number: Q59653
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: May 1, 2013
This is version 91 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